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2014

Section II
Insect Growth

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Chapter 8

The regulatory biosynthetic pathway of juvenile hormone

Zhentao Sheng1*, Raman Chandrasekar2

1

The Ben May Department for Cancer research, The University of Chicago, Chicago, IL, 60637,USA.
2
Department of Biochemistry & Molecular Biophysics, Kansas State University,
Manhattan, KS 66506, USA

Abstract

In this short review, it will be focused on the regulatory biosynthetic pathway of juvenile
hormone (JH). JH is involved in the regulation of nearly every aspect of insect life, such as
metamorphosis, reproduction, diapause, lifespan and polyphenisms. To perform these
biological functions, the biosynthesis of JH is under a rigorous control by insulin/TOR
signaling pathway, neuropeptides, neurotransmitters and other bioactive molecules, modulating
enzymes in the JH biosynthetic pathway. JH acid methyl transferase (JHAMT) converts JH acid
to JH or farnesoic acid (FA) to methyl farnesoate (MF) at final steps in JH biosynthesis.
JHAMT is the key regulatory enzyme for JH biosynthesis, which is activated by DPP-mediated
TGF signaling and also targeted by other regulators for JH biosynthesis. Targeting genes in JH
synthetic pathway, especially the late insect specific steps, was already broadly applied in studies
on JH function and is a promising strategy for pest control.
Key words: juvenile hormone, JH acid methyl transferase, Neuropeptides, Insulin/TOR signaling
pathway
*For Correspondence (email:

zsheng@uchicago.edu or zhtsheng911@gmail.com)

1. Introduction
Juvenile hormones (JH) are a family of insect sesquiterpenoids mainly
synthesized by the corpora allata (CA) (1) and also produced in the gonads, especially
the male accessory gland in Hyalophora cecropia, Apriona germari and Aedes
aegypti (reviewed in 2,3). To what extent do tissues other than CA work as sources
for JH biosynthesis should be easily determined by measuring the expression level
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Overview
1. Introduction
2. The regulatory biosynthetic pathway of JH
2a. Early steps
2b. Late steps
3. Regulators of JH biosynthesis
3a. Insulin / TOR nutrient signaling
3b. Neurotransmitters and neuropeptides
4. Conclusion and future direction
5. Acknowledgement
6. References

and the enzymatic activity of enzymes in the JH biosynthesis pathway. Structures of

major natural JHs (JH I, JH II, JH III, JH bisepoxide, JH III skipped bisepoxide) in
insects are shown in Fig.1, accompanied with their distribution (1, 4). The inactive
precursor of JH III, JH III acid (JHA) was also found in the hemolymph of some
insects, which was uptaken by gonads for the fulfillment of JH synthesis and then
transferred into the female during copulation with unknown roles (3, 5, 6). But
another JH precursor, methyl farnesoate (MF) found in the hemolymph of Diploptera
punctata and Drosophila melanogaster shows functional roles in pupation and
metamorphosis (1, 7-10) as well as it works as a reproduction regulator in some
Crustacea (11). The structures of JHA and MF can be found in Fig. 2.

Fig. 1. Structures and distributions of most natural juvenile hormones (JH).

Methoprene is one mostly used JH mimic.

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Fig. 2. JH biosynthetic pathway

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Despite its multiple functions, the molecular basis of JH action was unknown
until recently. New studies had established that the binding of JH to the bHLH-PAS
family transcription factor, methoprene-tolerant (Met) help the heterodimerization of
Met with other members of this family including steroid receptor coactivator (SRC),
Cycle and Clock, which in turn binds to the JH response elements (JHRE) present in
the promoters of JH-response genes. Even these studies defined Met as the JH
receptor, it is still poorly understood about the way JH produces lots of functional
outputs, possibly through heterodimerization with different bHLH-PAS partners,
recruitment of other alternative transcription factors, crosstalk with insulin or other
canonical signaling pathways or affecting on epigenetic programming (1,4,6,12-19).
There are already several excellent reviews about the molecular basis for JH action (1,
4, 14). Therefore, I will focus on the regulatory biosynthetic pathway of JH, another
important aspect for controlling JH function, which is applied by insects and may be
used in pest control (20, 21).

2. The regulatory biosynthetic pathway of JH

The concentration of JH in the hemolymph is regulated mainly by its synthesis
and also partially by its degradation, secretion and sequestration (1,19). The control
of JH biosynthesis is carried out through modulating the expression level or the
enzymatic activity of enzymes in the JH biosynthesis pathway. Biosynthesis pathway
of JH III (a universal form found in almost all insect species), showed in Fig.2,
consists of the universal mevalonate pathway and following insect specific steps. The
early steps of JH synthesis, before the formation of farnesyl diphosphate, are identical
to those of cholesterol synthesis in mammals (22). Taking advantage of the genome
sequencing and CA transcriptomics studies, cDNAs of all the JH biosynthesis
enzymes were cloned or can be obtained from Bombyx mori, D. melenogaster,
Anopheles gambiae, A. aegypti and Tribolium castaneum (22-29). Genes encoding JH
biosynthetic enzymes are predominantly or at least abundantly expressed in the CA
(24-26,28-31), indicating that CA is a highly specialized organ for isoprenoid
production and JH biosynthesis via the mevalonic acid pathway (22). In B. mori,
CA-specific transcriptional levels of the mevalonate enzymes display a coordinated
variations in parallel with JH biosynthesis in 4th and 5th instar larvae except for pupa
stage, where transcriptional levels of acetoacetyl-CoA thiolase (AACT),
3-hydroxy-3-methyl-glutaryl-CoA (HMG-CoA) reductase (HMGR), HMG-CoA
synthase (HMGS), Farnesyl pyrophosphate synthetase 1 (FPPS1) and FPPS3 are high
but JH synthesis is absent (24). And there was also a coordinated expression of all the
JH biosynthetic enzymes, which is correlated with dynamic changes of JH
biosynthesis in female pupae and adult mosquito (29). Increased JH biosynthesis
activity was observed in B. mori after last larval ecdysis when fed with artificial diet
added with 20-hydroxyecdysone (20E). Some unknown factors from the
20E-activated brain contribute to the stimulated JH biosynthesis by regulating the
expression of JH acid methyl transferase (JHAMT) and HMGR (32). These studies
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showed that JH biosynthetic enzymes are regulated at the transcriptional level,

resulting in the developmental changes of JH biosynthetic activity.
2a. Early steps
HMGR is the rate-limiting enzyme for the synthesis of mevalonic acid and
cholesterol in mammals (33,34). But there is less correlation between the enzymatic
activity or mRNA expression level of HMGR and the JH biosynthesis in D. punctata
(35) and B. mori (24), from which it is implicated that HMGR does not play a critical
role in the instant regulation of JH synthesis. However, the high expression level of
mevalonate enzymes, including HMGR, in the JH-absent pupae stage, definitely
provide plenty of precursors for the thereafter burst of JH biosynthesis when adult
emerged (24). RNAi of TOR (target of rapamycin) decreased JH synthesis and did
reduce the expression level of HMGR and HMGS in Blattella germanica and
A. aegypti (36,37). An anti-juvenile hormone agent, ethyl 4-(2-benzylhexyloxy)
benzoate, KF-13, inhibits juvenile hormone synthesis through the suppression of the
transcription of HMGR and HMGS in the CA in B. mori (38). JH synthesis by the CA
was progressively increased in vitro by the addition of exogenous precursors such as
geranyl-diphosphate, farnesyl-diphosphate, farnesol, farnesal and farnesoic acid (FA)
(29). So adequate precursors produced through the mevalonate pathway are
prerequisite for JH biosynthesis and its temporal regulation. Interestingly, the increase
of the JH biosynthesis by adding of FA is far higher than adding other precursors (29),
implicating that the methylation of FA or JHA by JHAMT is the instant regulatory
step for JH biosynthesis, where the substrate concentration and the enzyme activity
are both important for the rate of JH production. Or the step that catalyzes the
formation of FA may be the rate-limiting as suggested in this original study (29).
Steps of the mevalonate pathway are unlikely the rate-limiting or key regulatory steps
for JH biosynthesis. In conclusion, mevalonate enzymes including HMGR are
involved in the regulation of CA capability but not the immediate control for JH
synthesis by producing plenty of JH precursors in insects.
2b. Late steps
The later steps from farnesol to JH are unique to insects and some plants (22).
Due to the insect specificity, enzymes in later steps are more important in the
immediate regulation of JH biosynthesis and more suitable as targets for pest control
(21). Also due to their insect specificity, these enzymes were just recently
characterized including farnesyl diphosphate pyophosphatase (FPPP), farnesol
dehydronase (FOLD), farnesyl dehydrogenase (FALD), methyl farnesoate epoxidase
(MFO), farnesoic acid epoxidase (FAO) and JH acid methyl transferase (JHAMT)
(25,26,28,39-42). The last two steps of JH biosynthesis, the methylation of FA or JHA
and the expoxidation of MF or FA, are most likely exclusive for JH biosynthesis and
therefore the enzymes involved (JHAMT, MFO an FAO) are CA specific expressed.
In contrast, other enzymes in the late pathway, such as the FPPP, FOLD, and FALD
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are broadly expressed in many tissues, because farnesol and farnesal homeostasis are
vital for cells in majority of insects tissues. FPPP was first isolated from
D. melanogaster (40) and its homologue was recently characterized in A. aegypti (41).
All three identified A. aegypti FPPases (AaFPPase) are abundantly expressed in the
CA, but only AaFPPase-1 and -2 can functionally convert FPP to farnesol and only
the reduction of AaFPPase-1 by RNAi caused a significant decrease on JH
biosynthesis, implying AaFPPase-1 is the real FPPase involved in JH biosynthesis
(41). FOLD, oxidizing farnesol into farnesal, is a NADP+ dependent short-chain
dehydrodenase, first identified from A.aegypti. FOLD is expressed not only in the
CA but showing an expression pattern correlated with the JH synthesis level after
adult emergence (39). This study suggested that the oxidation of farnesol might be a
regulatory step in JH synthesis in adult mosquitoes. NAD+ dependent long-chain
aldehyde dehydrogenase 3 (ALDH3), working as a FALD, converts farnesal into
farnesoic acid in the mosquito CA (42). The knockdown of the expression of ALDH3
abolished the FALD enzyme activity and impaired JH biosynthesis (42). This study
functionally characterized ALDH3 as FALD in A. aegypti. The CYP15, belonging to
P450 family, catalyzes the expoxidization of FA in Lepidoptera or MF in other insect
species based on their substrate specificity, resulting in the variation of the last two
steps of JH (Fig.2) biosynthesis in insects (25,26,43,44). CYP15A1, from D. punctata,
specifically converts MF to JH III, not using various other MF-related compounds
such as farnesol, FA and farnesyl methyl ether as substrates. CYP15A1 is specifically
expressed in the CA and only during peak JH production.
Interestingly, selected 1,5-disubstituted imidazoles, known to inhibit JH
biosynthesis and cause accumulation of MF in cockroach CA, displayed parallel
effectiveness in inhibiting the activity of recombinant CYP15A1 and in vitro JH
biosynthesis by isolated CA (25). CYP15C1, cloned from B. mori, is also CA-specific
but converting FA to JHA in a highly stereospecific manner. CYP15C1 was
constitutively expressed from larval to adult stages, suggesting that the transcriptional
regulation of CYP15C1 is not important for the temporal regulation of JH production
in B. mori. JHAMT, responsible for the adding of methyl group to JHA or FA, was
first cloned from B. mori and appears critical for metamorphosis. At the beginning of
the fifth instar, the expression of JHAMT in CA reaches the highest level then
declines rapidly to undetectable by day 4 and remains so until pupation (28). During
the period of adult emergence, a high expression level of JHAMT was also observed
in female CA (24, 30).The expression pattern of JHAMT during the postembryonic
development exhibits a good correlation with JH synthesis by CA (45). In M. sexta,
B. mori and Samia cynthica ricini, only CA of female adults synthesizes JH, while
male CA produces JH acid (JHA). The authors believed it was because female, but
not male, CA, has JHAMT activity (24,30,46). Cause MF but not JHA or FA showed
functional activity, JHAMT mediated methylation should be more important than the
CYP15 catalyzed epoxidation for the regulation of JH biosynthesis and insect life
cycle. The JH-deficient CYP15C1 null mutant silkworm undergoes a precocious
metamorphosis with fewer larvallarval molts, which is because the possible presence
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of MF (26). Finally, it is reasonable to propose that enzymes of the late steps, if

controllable like JHAMT at transcriptional level or posttranscriptional level, are more
critical than that of early universal steps in the instant regulation of JH synthesis and
also more valuable to be targeted during chemical selection for pest control.

3. Regulators of JH biosynthesis
3a. Insulin/TOR Nutrient signaling
During the control of life span, reproductive maturation, reproductive diapause
and caste fate, nutrient status and nutritional signaling pathway, insulin/TOR pathway,
affects the JH biosynthesis by regulating the expression of genes in the JH
biosynthesis pathway. In D. melanogaster, the mutant of insulin receptor (InR)
yielded dwarf females with extended lifespan. These insects exhibited decreased JH
levels and undeveloped ovarioles that resembled the ovarioles of wild-type flies that
are in diapause, a delay in development in response to adverse environmental
conditions (47). An exogenous application of JH analog methoprene to InR mutant
dwarf females initiated vitellogenesis and restored lifespan similar to that of
wild-type flies (47). The A. aegypti larvae reared in inadequate nutrient conditions
developed into smaller adults and showed an inactivated TOR pathway, lower JH
levels, and needed additional blood meals to complete gonadotropic cycle (48).
Application of JH III to these small mosquitoes could initiate vitellogenesis with only
one blood meal (48). RNA interference (RNAi)-mediated gene knockdown of IRS
(InR substrate) and TOR abolished a JH peak and resulted in a worker phenotype in
larvae reared on queen diet which is destined to queen development (49). Recently, in
B. germanica, FOXO was shown to inhibit JH biosynthesis without modifying the
expression of HMGS1, HMGS2, HMGR or MFO (CYP15A1) in the CA (50). But it
is shown that TOR mediated nutrition status affects JH levels in this insect by
modulating the expression of HMGS1, HMGS2 and HMGR (36). The expression of
genes encoding JH biosynthetic enzymes (HMGS, HMGR, IPPI, FPPS, JHAMT and
MFO) is decreased and the JH biosynthesis is reduced when rapamycin, RNAi
against TOR, and PI3K inhibitor were applied in an in vitro culture of CC-CA
complex in A. aegypti (51). The transcriptional level of HMGR in CA of
D. melanogaster is also modulated by the insulin signal transduction pathway and a
transcriptional factor sterol regulatory element binding protein (SREBP) (52).
3b. Neurotransmitters and Neuropeptides
Neurotransmitters, such as dopamine and glutamate, were shown to regulate the
JH biosynthesis by the isolated CA in vitro (53,54). Studies in cockroach and
Drosophila revealed that glutamatergic nerves innervate CA cells and that the
N-methyl-D-aspartate subtype of glutamate receptors (NMDAR) are expressed in
both brain and CA (54). A recent study well established the molecular mechanisms of
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glutamate regulated JH biosynthesis, in which the transforming growth factor beta

(TGF) signaling plays a critical role (55). Glutamate binds to its receptor, NMDAR,
and then promotes the expression of TGF-like ligand decapentaplegic (Dpp) in the
CA, which stimulates JH biosynthesis through TGF signaling by upregulating
JHAMT transcription. Reduced Dpp and JHAMT expression was also detected in
larvae mutant for NMDAR (55). Because JHAMT is the key regulatory enzyme in JH
biosynthesis, it is important to study if TGF signaling plays a similar role in other
regulators or nutrient mediated regulation of JH biosynthesis. Even it has long been
known that dopamine is a suppressor, sometimes stimulator of the JH synthesis in the
CA in Manduca and Drosophila, the molecular mechanism is still elusive: receptor is
clear but downstream mechanism is unknown (53-62). Dopamine receptors are
divided into two subfamilies: D1-like activator and D2-like inhibitory receptors,
working through stimulatory and inhibitory G proteins respectively (55). In D.
melanogaster, the activation of D1-like receptors stimulates the synthesis of JH (57),
whereas the inactivation of these receptors, conversely, suppresses the JH synthesis
(58). When the expression of D2-like receptor was decreased by RNAi, the JH
biosyntheis is upregulated, suggesting that the DA inhibiting effect on the JH
synthesis in D. melanogaster is mediated at least in part via D2-like receptors (59).
The level of D1-like receptor expression in CA is much higher in the younger than in
the mature females, whereas D2-like receptor expression is much higher in the mature
than in the young females (60). D1-like receptors were also cloned and studied in
B. mori (61, 62). Based on current evidence, the effects of DA on JH biosynthesis has
not been fully understood.
JH biosynthesis is also regulated by both stimulatory (allatotropin, AT) and
inhibitory (allatostatin, AST) neuropeptides. These allatoregulatory neuropeptides
may reach CA via the hemolymph and/or via nervous connections, and regulate JH
synthesis in many insect species (63-65). The lepidopteran AT (Manse-AT;
GFKNVEMMTARGF-NH2) and AST (Manse-AST; pEVRFRQCYFNPISCF) were
both first isolated from the Manduca sexta (66, 67) and their encoding genes were
subsequently cloned (68, 69). Manse-AT, is the only one identified group of AT in
insects till now. Besides Manse-AST, there are two other types of AST:
YXFGL-NH2-AST family, W2W9-AST family (63-65). Manse-AT transcript
undergoes alternative splicing that is developmentally regulated in a tissue-specific
pattern and affected by starvation and mating (70-72). The stimulatory role of these
AT peptides in the regulation of JH synthesis is conserved in Lepidoptera and some
other Holometabola (65,73,74). Similarly, the inhibitory effect of Manse-AST on the
CA was demonstrated mainly in many Lepidoptera and the dipteran species
A. aegypti (65). The YXFGL-NH2-AST occurs in many orders of insects, but it
inhibits the JH synthesis by CA only in cockroaches, crickets, and termites (64).
W2W9-AST was found in crickets, which was originally isolated as a myoinhibitory
peptide and also was shown with prothoracicostatic activity (64). In contrast to their
known function as regulators for JH biosynthesis, it is very little known about the
molecular basis for AT and AST action. Recently, one neuropeptide G protein coupled
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receptor (NGPR), BNGR-A16, was first identified as the AT receptor in silkworm (75),
by comprehensive cloning and systematic analyses of all neuropeptide G protein
coupled receptors (GPCRs). Interestingly, BNGR-A16 was not highly expressed in the
CA, but instead was predominantly transcribed in the corpora cardiaca (CC), an organ
adjacent to the CA. Furthermore, Yamanaka and coauthors (75) purified and
characterized novel allatoregulatory peptides produced in AT receptor-expressing CC
cells, which may mediate the indirect effect of AT on the CA. These novel
allatoregulatory peptides belong to the short neuropeptide F (sNPF) family, showing
clearly inhibition of JH synthesis in an in vitro CA culture (75). Receptors of sNPF
are also GPCRs: BNGR-A10 and A11 in silkworm, and so do the receptor for
Manse-AST: BNGR-A1 in silkworm and Drostar1 and 2 in D. melanogaster (75, 76).
sNPF suppressed the expression of MVAK and HMGR, and Manse-AST suppressed
the expression of MVAK, HMGR and IPPI, which were initially believed to inhibit
JH synthesis by blocking the transfer or cleavage of citrate to yield of acetyl-CoA
(53). So neuropeptide GPCRs and their peptide ligands, including AT, AST and sNPF,
play a critical role in the control of JH biosynthesis by modulating the expression of
JH biosynthesis enzymes. But it is still not clear how neuropeptide GPCRs regulate,
stimulate or inhibit JH biosynthesis enzymes at transcriptional level.
AT receptors were also isolated from A. aegypti, T. castaneum and M. sexta.
Based on their expression patterns, the working model of AT receptors maybe not the
same in different insect species and the function of AT and its receptors is not only to
stimulate the biosynthesis of JH (77-79). Unlike the CC-specific expression pattern of
AT receptor in B. mori, the A. aegypti AT receptor was expressed in the CA but not
the CC, showing a expression pattern resembles the changes in JH biosynthesis (77).
Besides the presumable expression in the CA (showed with the expression in the
head), the T. castaneum AT receptor was surprisingly highly expressed in
reproductive system with a higher level in the male (78). Whereas in M.sexta AT
receptor was expressed in multiple tissues in feeding larvae, the highest level is in the
Malphighian tubules (79).

4. Conclusion and Future directions

The JH biosynthesis pathway is broadly regulated, especially at the
transcriptional level of enzymes. The early steps, belonging to the universal
mevalonate pathway, are important for the regulation of CA capacity for JH synthesis,
but not the instant control of JH production. On the other hand the late insect specific
steps are critical for the temporal regulation of JH biosynthesis, also promising for
pest control by screening for small chemicals or bioactive molecules that specifically
decreased the transcriptional level or enzymatic activity of JH biosynthesis enzymes.
The transcriptome analysis is an useful method to unveil the molecular basis for most
of the known regulators of JH biosynthesis, using microarray or mRNA sequencing.
For regulators that do not affect JH biosynthesis enzymes at the transcriptional level,
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it is necessary to investigate their effects on the enzyme activity and measure their
influence on JH biosynthetic capability by analyzing the changes of JH precursor
pools (42, 80).

5. Acknowledgements
The authors thanks to Drs. Sheng Li, Chinese Academy of Sciences, China, and
Prof. Noriega, F.G., Florida National University, USA and Dr. Hua Bai, Brown
University, USA for their critical readings and valuable comments.

6. References
1.
2.
3.
4.
5.
6.
7.
8.
9.
10.
11.
12.
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14. Riddiford, L.M. (2012) How does juvenile hormone control insect metamorphosis and reproduction?.
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20. Cusson, M., Sen, S.E., and Shinoda T. (2013) Juvenile hormone biosynthetic enzymes as targets for
insecticide discovery. Advanced Technologies for Managing Insect Pests. Springer Netherlands, 31-55.
21. Palli, S.R. and Cusson, M. (2007) Future insecticides targeting genes involved in the regulation of molting
and metamorphosis. Insecticides Design Using Advanced Technologies. Springer Berlin Heidelberg,
pp.105-134.
22. Belle s, X., Martin, D., Piulachs, M.D. (2005) The mevalonate pathway and the synthesis of juvenile
hormone in insects. Annu. Rev. Entomol. 50:181199
23. Liu, Y., Sheng, Z.T., Jiang, R.J., Cao, M.X., Li, S. (2007) Progress in juvenile hormone synthesis. Acta
Entomologica Sinica. 50(12): 1285-1292.
24. Kinjoh, T., Kaneko, Y., Itoyama, K., Mita, K., Hiruma, K. and Shinoda, T. (2007) Control of juvenile
hormone biosynthesis in Bombyx mori: Cloning of the enzymes in the mevalonate pathway and
assessment of their developmental expression in the corpora allata. Insect Biochem. Mol. Biol. 37(8):
808-818.
25. Helvig, C., Koener, J.F., Unnithan, G.C., Feyereisen, R. (2004) CYP15A1, the cytochrome P450 that
catalyzes epoxidation of methyl farnesoate to juvenile hormone III in cockroach corpora allata. Proc.
Natl. Acad. Sci. USA 101: 402429.
26. Daimon, T., Kozaki, T., Niwa, R., Kobayashi, I., Furuta, K., et al., (2012) Precocious Metamorphosis in
the Juvenile HormoneDeficient Mutant of the Silkworm, Bombyx mori. PLoS genetics 8 (3): e1002486.
27. Noriega, F.G., Ribeiro, J.M., Koener, J.F., Valenzuela, J.G., Hernandez-Martnez, S., Pham, V.M.,
Feyereisen, R. (2006) Comparative genomics of insect juvenile hormone biosynthesis. Insect Biochem
Mol Biol. 36(4): 366-374.
28. Shinoda, T. and Itoyama, K. (2003) Juvenile hormone acid methyltransferase: a key regulatory enzyme
for insect metamorphosis. Proc. Natl. Acad. Sci. 100(21): 11986-11991.
29. Nouzova, M., Edwards, M.J., Mayoral, J.G., Noriega, F.G. (2011) A coordinated expression of
biosynthetic enzymes controls the flux of juvenile hormone precursors in the corpora allata of mosquitoes.
Insect Biochem. Mol. Biol. 41(9): 660-669.
30. Sheng, Z., Ma, L., Cao, M.X., Jiang, R.J., Li, S. (2008) Juvenile hormone acid methyl transferase is a key
regulatory enzyme for juvenile hormone synthesis in the Eri silkworm, Samia cynthica ricini. Arch. Insect
Biochem. Physiol. 69(3): 143-154.
31. Hiroto, U., Shinoda, T. and Hiruma, K. (2009) Spatial expression of the mevalonate enzymes involved in
juvenile hormone biosynthesis in the corpora allata in Bombyx mori. J. Insect Physiol. 55(9): 798-804.
32. Kaneko,Y., Kinjoh, T., Kiuchi, M. and Hiruma, K. (2011) Stage-specific regulation of juvenile hormone
biosynthesis by ecdysteroid in Bombyx mori. Mol. Cell. Endocrinol. 335(2): 204-210.
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33. Goldstein, J.L., Brown, M.S. (1990) Regulation of the mevalonate pathway. Nature 343:425430.
34. Goldstein, J.L., Brown, M.S. (1997) The low-density lipoprotein pathways and its relation to atherosclerosis. Annu. Rev. Biochem. 46:897930.
35. Feyereisen, R., Farnsworth, D.E. (1987) Characterization and regulation of HMG-CoA reductase during a
cycle of juvenile hormone synthesis. Mol. Cell. Endocrinol. 53:227238.
36. Maestro, J.L., Cobo, J., and Bells, X. (2009) Target of rapamycin (TOR) mediates the transduction of
nutritional signals into juvenile hormone production. J. Biol. Chem. 284:55065513.
37. Prez-Hedo, Meritxell, Crisalejandra Rivera-Perez, and Noriega, F.G. (2013) The insulin/TOR signal
transduction pathway is involved in the nutritional regulation of juvenile hormone synthesis in Aedes
aegypti. Insect Biochem. Mol. Biol. 43(6):495-500.
38. Kaneko, Y., Furuta, K., Kuwano, E., Hiruma, K. (2011) An anti-juvenile hormone agent, ethyl
4-(2-benzylhexyloxy) benzoate, inhibits juvenile hormone synthesis through the suppression of the
transcription of juvenile hormone biosynthetic enzymes in the corpora allata in Bombyx mori. Insect
Biochem. Mol. Biol. 41(10): 788-794.
39. Mayoral, J.G., Nouzova, M., Navare, A., Noriega, F.G. (2009) NADP+-dependent farnesol
dehydrogenase, a corpora allata enzyme involved in juvenile hormone synthesis. Proc. Natl. Acad. Sci.
106(50): 21091-21096.
40. Cao, Li, Ping Zhang and David F. Grant (2009) An insect farnesyl phosphatase homologous to the
N-terminal domain of soluble epoxide hydrolase. Biochemical and Biophysical Research Communication
380 (1): 188-192.
41. Nyati, Partial et al. (2013) Farnesyl phosphatase, a corpora allata enzyme involved in Juvenile hormone
biosynthesis in Aedes aegypti. PLoS One 8.8: e71967.
42. Rivera-Perez, C., Nouzova, M., Clifton, ME., Martin Garcia, E., LeBlanc, E., Noriega, FG. (2013)
Aldehyde dehydrogenase 3 converts farnesal into farnesoic acid in the corpora allata of mosquitoes. Insect
Biochem. Molec. Biol. 43: 675-682.
43. Daimon, T. and Shinoda, T. (2013) Function, diversity, and application of insect juvenile hormone
epoxidase (CYP15). Biotechnol. Applied Biochem. 60 (1): 82-91.
44. Defelipe, L. A., Dolghih, E., Roitberg, A.E. Nouzova, M., Mayoral, J.G., Noriega, F.G., and Turjanski.
A.G., (2011) Juvenile hormone synthesis: esterify then epoxidize or epoxidize then esterify? Insights
from the structural characterization of juvenile hormone acid methyltransferase. Insect Biochem. Mol.
Biol. 41(4): 228-235.
45. Niimi, S., Sakurai, S. (1997) Developmental changes in juvenile hormone and juvenile hormone acid
titers in the hemolymph and in vitro juvenile hormone synthesis by corpora allata of the silkworm,
Bombyx mori. J. Insect Physiol. 43: 875884.
46. Bhaskaran, G., Sparagana, S.P., Barrera, P., Dahm, K.H. (1986) Change in corpus allatum function during
metamorphosis of the tobacco hornworm Manduca sexta: regulation at the terminal step in juvenile
hormone biosynthesis. Arch. Insect Biochem. Physiol. 3: 321338.
47. Tatar, M., Kopelman, A., Epstein, D., Tu, M. P., Yin, C.M., and Garofalo, R.S. (2001) A mutant
Drosophila insulin receptor homolog that extends life-span and impairs neuroendocrine function. Science
292: 107110.
48. Shiao, S. H., Hansen, I. A., Zhu, J., Sieglaff, D. H., and Raikhel, A. S. (2008) Juvenile hormone connects
larval nutrition with target of rapamycin signaling in the mosquito Aedes aegypti. J. Insect Physiol. 54:
231239.
49. Mutti, N.S., et al. (2011) IRS and TOR nutrient-signaling pathways act via juvenile hormone to influence
honey bee caste fate. J. Experimental Biol. 214(23): 3977-3984.
50. Sren-Castillo, S., Abrisqueta, M., and Maestro, J.L. (2012) FoxO inhibits juvenile hormone biosynthesis
and vitellogenin production in the German cockroach. Insect Biochem. Mol. Biol. 42(7):491-498.
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51. Perez-Hedo, M., Rivera-Perez, C., Noriega, F.G. (2013) The insulin/TOR signal transduction pathway is
involved in the nutritional regulation of juvenile hormone synthesis in Aedes aegypti. Insect Bicohem.
Mol.Biol. IB2448_proof 29 March 2013 -1/6 (in press).
52. Belgacem, Y.H., Martin, J-R. (2007) Hmgcr in the corpus allatum controls sexual dimorphism of
locomotor activity and body size via the insulin pathway in Drosophila. PLOS ONE 1 e187.
53. Kiyoshi, H. and Kaneko. Y. (2013) Hormonal regulation of insect metamorphosis with special reference
to juvenile hormone biosynthesis. Current Topics in Developmental Biol. 103: 73.
54. Chiang, A.S., Lin, W.Y., Liu, H.P., Pszczolkowski, M.A., Fu, T.F., Chiu, S.L., Holbrook, G.L. (2002)
Insect NMDA receptors mediate juvenile hormone biosynthesis. Proc. Natl. Acad. Sci. 99(1): 37-42.
55. Huang, J., Tian, L., Peng, C., Abdou, M., Di Wen, Wang, Y., Li, S. and Wang, J. (2011) DPP-mediated
TGF signaling regulates juvenile hormone biosynthesis by activating the expression of juvenile hormone
acid methyltransferase. Development 138(11): 2283-2291.
56. Daniela, V., Picetti, R., and Borrelli, E. (2000) Structure and function of dopamine receptors.
Neuroscience & Biobehavioral Rev. 24(1): 125-132.
57. Rauschenbach, I.Y., Bogomolova, E.V., Karpova, E.K., Shumnaya, L.V., Gruntenko, N.E. (2012) The
role of D1 like receptors in the regulation of juvenile hormone synthesis in Drosophila females with
increased dopamine level. Dokl. Biol. Sci. 441(4): 393395.
58. Karpova, E.K., Bogomolova, E.V., Romanova, I.V., Gruntenko, N.E., Yu Rauschenbach, I. (2012)
Role of DopR in the molecular mechanism of the dopamine control of juvenile hormone metabolism in
female Drosophila. Russ. J. Genet. 48(7): 9991022.
59. Gruntenko, N.E., Laukhinaa, O.V., Bogomolovaa, E.V., Karpovaa, E.K., Menshanova, P.N. and
Romanovab, I.V. (2012) Downregulation of the dopamine D2-like receptor in corpus allatum affects
juvenile hormone synthesis in Drosophila melanogaster females. J. Insect Physiol. 58(3): 348-355.
60. Gruntenko, N.E., Laukhina, O.V. and Rauschenbach, I.Y. (2012) Role of D1-And D2-Like Receptors in
Age-Specific Regulation of Juvenile Hormone and 20-Hydroxyecdysone Levels by Dopamine In
Drosophila. J. Insect Physiol. 58(12):1534-1540.
61. Ohta, H., Tsuchihara, K., Mitsumasu, K., Yaginuma, T., Ozoe, Y., Asaoka, K. (2009) Comparative
pharmacology of two D1-like dopamine receptors cloned from the silkworm Bombyx mori. Insect
Biochem. Mol. Biol. 39(5): 342-347.
62. Mitsumasu, K., Ohta, H., Tsuchihara, K., Asaoka, K., Ozoe, Y., Niimi, T., Yamashita, O., Yaginuma, T.
(2008) Molecular cloning and characterization of cDNAs encoding dopamine receptor1 and2 from
brainsuboesophageal ganglion of the silkworm, Bombyx mori. Insect Mol. Biol. 17(2): 185-195.
63. Barbara, S. (2000) A review of the role of neurosecretion in the control of juvenile hormone synthesis: a
tribute to Berta Scharrer. Insect Biochem. Mole. Biology 30: 653-662.
64. Barbara, S. and Tobe, S.S. (2007) The role of allatostatins in juvenile hormone synthesis in insects and
crustaceans. Annu. Rev. Entomol. 52: 277-299.
65. Gde, G., and Hoffmann, K.H. (2005) Neuropeptides regulating development and reproduction in insects.
Physiol. Entomol. 30(2): 103-121.
66. Kataoka, H., Toschi, A., Li, J.P., Carney, R.L., Schooley, D.A., and Kramer, S.J. (1989). Identification of
an allatotropin from adult Manduca sexta. Science, 243(4897): 1481-1483.
67. Kramer, S.J., Toschi, A., Miller, C.A., Kataoka, H., Quistad, G.B., Li, J.P., Carney, R.L., and
Schooley, D.A. (1991) Identification of an allatostatin from the tobacco hornworm Manduca sexta. Proc.
Natl. Acad. Sci. 88(21): 9458-9462.
68. Taylor, P.A., Bhatt, T.R., and Horodyski, F.M. (1996) Molecular characterization and expression analysis
of Manduca sexta allatotropin. Euro. J. Biochem. 239(3): 588-596.
69. Jansons, I.S., Cusson, M., Mcneil, J.N., Tobe, S.S., Bendena, W.G. (1996) Molecular characterization of a
cDNA from Pseudaletia unipuncta encoding the Manduca sexta allatostatin peptide (Mas-AST). Insect
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Biochem. Mol. Biol. 26 (8): 767-773.

70. Sheng, Z., Ma, L., Cao, M.X., Li, S., and Jiang, R.J. (2007). Biochemical and molecular characterization
of allatotropin and allatostatin from the Eri silkworm, Samia cynthia ricini. Insect Biochem. Mol. Biol.
37(1): 90-96.
71. Kyeong-Yeoll, L., and Horodyski, F.M., (2006) Effects of starvation and mating on corpora allata activity
and allatotropin (Manse-AT) gene expression in Manduca sexta. Peptides 27(3): 567-574.
72. Abdel-Latief, M., Meyering-Vos, M., and Hoffmann, K.H., (2003) Molecular characterisation of cDNAs
from the fall armyworm Spodoptera frugiperda encoding Manduca sexta allatotropin and allatostatin
preprohormone peptides. Insect Biochem. Mol. Biol. 33 (2): 467-476.
73. Elekonich, M.M., and Horodyski, F.M. (2003) Insect allatotropins belong to a family of structurallyrelated myoactive peptides present in several invertebrate phyla. Peptides 24(10): 1623-1632.
74. Griebler, M., Westerlund, S.A., Hoffmann, K.H., Meyering-Vos, M. (2008) RNA interference with the
allatoregulating neuropeptide genes from the fall armyworm Spodoptera frugiperda and its effects on the
JH titer in the hemolymph. J. Insect Physiol. 54(6):997-1007.
75. Yamanaka, N., Yamamoto, S., Duan itan, Watanabe, K., Kawada, T., et al., (2008) Neuropeptide
receptor transcriptome reveals unidentified neuroendocrine pathways. PLoS One 3(8): e3048.
76. Kreienkamp, H.J, Larusson, H.J., Witte, I., Roeder, T., Birgul, N., Honck, H.H., Harder, S., Ellinghausen,
G., Buck, F., Richter, D. (2002) Functional annotation of two orphan G-protein-coupled receptors,
Drostar1 and-2, from Drosophila melanogaster and their ligands by reverse pharmacology. J. Biological
Chem. 277 (42): 39937-39943.
77. Nouzova, Marcela, et al. (2012) Functional characterization of an allatoropin receptor expressed in the
corpora allata of mosquitoes. Peptides 34(1) 201-208.
78. Horodyski, F.M., Verlinden. H., Filkin, N., Vandersmissen, H.P., Fleury, C., Reynolds, S.E., Kai, Z.P,
Broeck. J.V. (2011) Isolation and functional characterizationof an allatropin receptor from Manduca
sexta. Insect Biochem. Mol. Biol. 41(10): 804-814.
79. Kristel, V., Heleen, V., Marleen, L., Jozef Vanden Broeck, Roger, H. (2011) Characterization of an
allatropin-like peptide receptor in the red flour beetle, Tribolium castaneum. Insect Biochem. Mol. Biol
41(10): 815-822.
80. Rivera-Perez, C., Nouzova, M., Noriega, F.G. (2012) A quantitative assay for the juvenile hormones and
their precursors using fluorescent tags. PLoS One, 7(8): e43784.
Article History: Received 15th May 2013; Revised 3rd September 2013 and Accepted 2nd Feburary 2014;
Published 30th October 2014.
Reviewed by: Noriega, F.G., Florida National University, USA

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Praying mantis

Photo Credit: Adrian Kozakiewicz

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2014

Section III

Insect Immunity

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Table Contents

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Page No.

Preface
Forward message
Contributors
Reviewers
Acknolwedgement

i
ii
iii
iv
v

Volume1
Section I: Insect Biochemical approaches

1. Introduction to Insect Molecular Biology.

Raman Chandrasekar, P.G., Brintha, Enoch Y.Park, Paolo Pelsoi, Fei Liu,
Marian Goldsmith, Anthony Ejiofor, B.R., Pittendrigh, Y.S., Han,
Fernando G. Noriega, Manickam Sugumaran, B.K., Tyagi, Zhong Zheng Gui,
Fang Zhu, Bharath Bhusan Patnaik, and P. Michailova

2.

Modulation of Botanicals on pests biochemistry.

57

Sahayaraj, K.

3.

Detoxication, stress and immune responses in insect antenna:

new insights from transcriptomics.

75

David Siaussat, Thomas Chertemps and Martine Maibeche

4.

Application of isotopically labeled compounds and tandem mass

spectrometry for studying metabolic pathways in mosquitoes.

99

Stacy Mazzalupo and PatriciaY.Scaraffia

5.

Field Response of Dendroctonus armandi Tsai & Li (Coleoptera:

Scolytinae) to Synthetic Semiochemicals in Shaanxi, China.

127

Shou-An Xie, Shu-Jie L.V., Hui-Chen, Raman Chandrasekar

xvii

Section II: Insect Growth

6. Insect Cuticular SclerotizationHardening Mechanisms and Enzymes.

149

Manickam Sugumaran

7. New Approaches to Study Juvenile Hormone Biosynthesis in Insects.

185

Crisalejandra Rivera-Perez, Marcela Nouzova and Fernando G. Noriega

8. The regulatory biosynthetic pathway of juvenile hormone.

217

Zhentao Sheng and Raman Chandrasekar

Section III:

Insect Immunity

9. The innate immune network in a hemimetabolous insect, the brown

planthopper, Nilaparvata lugens.

233

Yanyuan Bao, Raman Chandrasekar, Chuan-Xi Zhang

10. Immune Pathways in Anopheles gambiae.

253

Maria L. Simes and Raman Chandrasekar

11. Key biochemical markers in silkworms challenged with immuno-

271

elicitors and their association in genetic resistance for survival.

Somasundaram, P., Chandraskear, R., Kumar,K.A., and Manjula, A.

Section IV:

Insect Molecular Genetics

12. The recent progress of the W and Z chromosome studies of the

291

silkworm, Bombyx mori

Hiroaki Abe, Tsuguru Fujii and Raman Chandrasekar

13. Molecular characterization and DNA barcoding for identification of

317

agriculturally important insects.

Rakshit Ojha, Jalali, S.K., and Venkatesan, T.

14. Polytene chromosomes and their significance for Taxonomy,

331

Speciation and Genotoxicology

Paraskeva V. Michailova

15. Insect exuvium extracted DNA marker: a good complementary

molecular taxonomic characteristics with special reference
to mosquitoes.

355

Dhanenjeyan, K. J., Paramasivam, R., Thanmozhi, V., Chandrasekar,R., and Tyagi, B.K.
Index

363

xviii

Volume2
Section V:

Molecular Biology of Insect Pheromones

16. Understanding the functions of sex-peptide receptors?

373

Orly Hanin, Ada Rafaeli

17. Current views on the function and evolution of olfactory receptors

385

in Lepidoptera.

Arthur de Fouchier, Nicolas Montagn, Olivier Mirabeau, Emmanuelle Jacquin-Joly

18. Molecular architecture, phylogeny and biogeography of pheromone

409

biosynthesis and reception genes / proteins in Lepidoptera.

Jian-Cheng Chang, P. Malini, R. Srinivasan

Section VI:

Insect Molecular Biology

19. Application of Nanoparticles in sustainable Agriculture :

429

Its Current Status.

Atanu Bhattacharyya , Raman Chandrasekar, Asit Kumar Chandra,

Timothy T. Epidi and Prakasham, R.S.

20. Mosquito Ribonucleotide Reductase: A Site for Control.

449

Daphne Q.-D. Pham, Victor H. Perez, Lissette Velasquez, Dharty Bhakta,

Erica L. Berzin, Guoli Zhou, and Joy. J. Winzerling.

21. Green protocol for synthesis of metal nanoparticles

to control insect pests.

473

Murugan, K., Chandrasekar, R., Panneerselvam, C., Naresh Kumar, A.,

Madhiyazhagan, P., Mahesh Kumar, P., Jiang-Shiou Hwang, Jiang Wei

22. Aquaporins in Blood-Feeding Arthropods.

497

Lisa L. Drake, Hitoshi Tsujimoto, Immo A. Hansen

23. Mimetic analogs of three insect neuropeptide classes

509

for pest management.

Ronald J. Nachman

xix

Section VII:

Insect Pest Management through

Biochemical and Molecular approaches

24. Induced resistance in plants against insect pests and

533

counter-adaptation by insect pests.

Abdul Rashid War and Hari C Sharma

25. Insect Chemical communication - an important component of

549

novel approaches to insect pest management.

Usha Rani, P.

26. Mosquito control using biological larvicides: Current Scenario.

575

Subbiah Poopathi, C. Mani and R. Chandrasekar

27. Application of RNAi toward insecticide resistance management.

595

Fang Zhu, Yingjun Cui, Douglas B. Walsh, Laura C. Lavine

Section VIII:

Insect Bioinformatics

28. Entomo-informatics: A prelude to the concepts in Bioinformatics.

621

Habeeb, S.K.M. and Raman Chandrasekar

29. Molecular expression and structure-function relationships of

633

apolipophorin III in insects with special reference to innate immunity.

Bharat Bhusan Patnaik, Raman Chandrasekar, Yeon Soo Han

30. Computer-aided pesticide design: A short view

685

Jitrayut Jitonnom

Index

709

xx

ISBN No. 978-1-63315-205-2 (USA)

First Edition: Volume 1, 2 October 2014

Total No. Pages: 398 + 372 = 770

Edited by Raman Chandrasekar

B.K. Tyagi
Zhong Zheng Gui
Gerald R. Reeck
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Volume 1 & 2, October 2014

Short Views on Insect Biochemistry

and Molecular Biology

PREFACE
Entomology as a science of inter-depended branches like biochemistry, molecular entomology, insect
biotechnology; has made rapid progress in its attributes in the light of modern discoveries. This also
implies that there is an urgent need to manage the available resources scientifically for the good of man.
In the past five decades, entomology in the world/country has taken giant steps ahead. Continued
research has evolved better pest management through molecular approaches. The aim of the Short
Views on Insect Biochemistry and Molecular Biology book is to integrate perspectives across
biochemistry and molecular biology, physiology, immunology, molecular evolution, genetics,
developmental biology and reproduction of insects. This century is proclaimed as the Era of
Biotechnology and its consists of all types of Mol-Bio applications, which is an essential component for
a through understanding of the Insect Biology. This volume 1 & 2 (8 section with 30 chapters)
establishes a thorough understanding of physiological and biochemical functions of proteins, genes in
insects life processes; the topics dealt with in the individual chapters include chemistry of the insect
cuticle, hormone and growth regulators; biochemical defenses of insects; the biochemistry of the toxic
and detoxification action; modern molecular genetics and evolution; inter- and intra-specific chemical
communication and behavior; insect pheromone and molecular architecture, phylogeny and chemical
control of insect by using insect pheromones biotechnology; insect modern biology and novel plant
chemical and microbial insecticides for insect control, followed by a discussion of the various
mechanisms of resistance (both behavioral and physiological) and resistance management; modern insect
pest management through biochemical and molecular approaches; Mimetic analogs of insect
neuropeptide for pest management; entomo-informatics and computer-aided pesticide designing. In short
this book provides comprehensive reviews of recent research from various geographic areas around the
world and contributing authors area recognized experts (leading entomologist/scientist) in their
respective filed of molecular entomology. We will miss this collaboration now it has ended, but will feel
rewarded if this book is appreciated by our team/colleagues and remarkable mile stone in entomology
field.
This book emphasizes upon the need for and relevance of studying molecular aspects of entomology in
Universities, Agricultural Universities and other centers of molecular research. To encompass this
knowledge and, particularly disseminate it to the scientific community free of cost, was the major
inspiring force behind the launch of Short Views on Insect Biochemistry and Molecular Biology.

Editors

Raman Chandrasekar
Brij Kishore Tyagi

ii

iii

iv

vi

ShortViewson

InsectBiochemistryand
MolecularBiology
Editedby
Raman Chandrasekar, Ph.D.,
Kansas State University, USA.
B.K.Tyagi, Ph.D.,
Centre for Research in Medical Entomology (ICMR), India.
Zhong Zheng Gui, Ph.D.,
Jiangsu University of Science and Technology,
Sericultural Research Institute, Chinese Academy of
Agricultural Sciences, China.
Gerald R. Reeck, Ph.D.,
Kansas State University, USA.

vii

viii

SION
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Contributing Authors

Dr. B.K.Tyagi

Prof.Fernando G. Noriega

Centre for Research in Medical Entomology,

4Sarojini Street, Chinna Chokkikulam,
Madurai 625002 (TN), India

Department of Biological Sciences

HLS 227, Florida International University
11200 SW 8th St, Miami, FL 33199, USA.

Prof. Gui Zhongzheng

Dr. Zhentao Sheng

Sericultural Research Institute,

Chinese Academy of Agricultural
Sciences, Zhenjiang, 212018,
Jiangsu, P. R. China.

Chicogo University, Chicogo, USA.

Prof. K. Sahayaraj

Prof.Yanyuan Bao
Institute of Insect Science,
Zhejiang University, China.

Dept. of Advanced Zoology and Biotechnology,

St. Xavier's College
Palayamkottai 627 002, Tamil Nadu, India.

Prof. Chuan-Xi Zhang,

Prof. David Siaussat

Dr. Maria L. Simes

Universit Pierre et Marie Curie (Paris 6/UPMC),

UMR 1272A Physiologie de l'Insecte:
Signalisation et Communication (PISC),
7 Quai Saint Bernard, Batiment A - 4me tage bureau 410, 75252 Paris Cedex 05, France.

Prof. PatriciaY.Scaraffia
Department of Tropical Medicine,
Tulane University, New Orleans,
LA 70112, USA.

Prof. Shou-An Xie

Institute of Insect Science,

Zhejiang University, China.

UEI Parasitologia Mdica,

Centro de Malria e Outras Doenas Tropicais,
Instituto de Higiene e Medicina Tropical,
Rua da Junqueira 96, 1300 Lisboa,
Portugal.

Dr. P. Somasundaram
Central Sericultural Germplasm Resources Centre,
P.B.No.44, Thally Road,
Hosur-635109,
Tamilnadu, India.

College of Forestry,
Northwest A & F University
Yangling, Shaanxi 712100, China

Dr. Hiroaki Abe

Dr. Raman Chandrasekar

Dr. S.K. Jalali

Department of Biochemistry and Molecular

Biophysics, Kanas State University,
Manhattan, 66506, KS, USA.

Prof. Gerald R. Reeck

Department of Biochem. and Molecular
Biophyscis, Kansas State University, KS, USA.

Prof. Manickam Sugumaran

Department of Biology
University of Massachusetts Boston
100 Morrissey Blvd,
Boston, MA 02125, USA.

Tokyo University of Agriculture and Technology,

Japan.

National Bureau of Agriculturally Important

Insects, ICAR, India.

Prof. Paraskeva V. Michailova

Institute of Biodiversity and
Ecosystem Research,
1 Tzar Osvoboditel boulv
Bulgarian Academy of Sciences
Sofia 1000, Bulgaria.

Prof. Ada Rafaeli

Associate Director for Academic Affairs &
International Cooperation
Agricultural Research Organization,
The Volcani Center, P. O. Box 6,
Bet Dagan 50250, Iseral.

ix

Prof. Emmanuelle Jacquin-Joly

Dr. Fei Liu

UMR PISC Physiologie de l'insecte

INRA, Route de Saint-Cyr
78026 Versailles cedex, France..

Department of Biological Science & Technol.,

Shaanxi Xueqian Normal University,
Shaanxi, China.

Dr. R. Srinivasan

Prof. Marian Goldsmith

Entomologist and Head of Entomology Group

AVRDC-The World Vegetable Center
60 Yi Ming Liao, Shanhua
Tainan 74151, Taiwan.

Biological Sciences Department,

University of Rhode Island,
Kingston, RI 02881, USA

Prof. Atanu Bhattacharyya

Prof. Anthony Ejiofor

Vidyasagar College for Women,

Post Graduate Department of Environmental
Science,
University of Kolkata, India.

Department of Biological Sciences,

College of Agriculture, Human & Natural
Sciences, Tennessee State University,
3500 John A Merritt Blvd., Nashville,
Tennessee 37209, USA.

Prof. Daphne Q.-D. Pham

Dr. Bharath Bhusan Patnaik

Dept of Biological Sciences,

University of Wisconsin-Parkside,
900 Wood Road, Kensoha,
WI 53144, USA.

School of Biotechnology,
Trident Academy of Creative Technology
(TACT), Bhubaneswar 751013 Odisha, India.

Prof. Jitrayut Jitonnom

Prof. B.R. Pittendrigh

School of Science
University of Phayao, Thailand.

Department of Entomology,
University of Illinois, Urbana-Champaign, IL,
61801, USA
.

Prof. K. Murugan

Dr. Subbiah Poopathi

Department of Zoology, School of Life Sciences,

Bharathiar University,
Coimbatore - 641 046, India.

Prof. Immo A. Hansen

Department of Biology,
New Mexico State University,
Las Cruces, NM, USA.

Dr. Ronald J. Nachman

USDA-ARS,
Food Animal Protection Research Laboratory,
USA.

Dr. Hari C Sharma

International Crops Research Institute for the
Semi-Arid Tropics (ICRISAT), Patancheru502324,
Andhra Pradesh, India.

Prof. Paolo Pelsoi

State Key Laboratory for Biology Plant Diseases
and Insect Pests, Institute of Plant Protection,
Chinease Academy of Agricultural Sciences,
Bejing, China.

Unit of Microbiology and Immunology,

Vector Control Research Centre
(Indian Council of Medical Research),
Medical complex, Indira Nagar,
Puducherry 60 5006, India.

Dr. P.Usha Rani

Biology and Biotechnology Division
Indian Institute of Chemical Technology
(CSIR)Taranaka,
Hyderabad - 500 007 (AP), India.

Dr. Fang Zhu

Irrigated Agriculture Research and Extension
Center, Dept.of Entomology,
Washington State University,
Prosser, WA, USA.

Prof. S.K.M. Habeeb

Department of Bioinformatics,
Faculty of Engineering & Technology,
SRM University, Kattankulathur,
Chennai 603203, Tamilnadu, India.

Prof. Yeon Soo Han

Division of Plant Biotechnology,
College of Agriculture & Life Science,
Chonnam National University,
Gwangju 500-757, South Korea

SION
MIS

TERNA
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N AL B OO

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Reviewer & External supportive members

Prof. Michael Riehle, Department of Entomology, University of Arizona, USA.

Dr. Dawn L.Geiser, College of Agriculture and Life Sciences, University of Arizona, USA.
Prof. Young Jung Kwon, School of Applied Biosci., Kyungpook National University, South Korea.
Dr. Kaliappandar Nellaiappan, CuriRx Inc. USA.
Prof. Patricia Y. Scaraffia, Department of Tropical Medicine, Tulane University, USA.
Prof. Richard Newcomb, Plant & Food Research, University of Auckland, New Zealand.
Dr. S. Krishnaswamy, School of Biotechnology, Madurai Kamaraj University, South India.
Dr. Mary-Anne Hartley, University of Lausanne, Switzerland.
Dr. Igor F. Zhimulev, Institute of Molecular and Cellular Biology, Novosibirsk, Russia.
Dr. S. Subramanin, Indian Agricultural Research Institute. India.
Prof. Gustavo F. Martins, Departament de Biologia Geral, Universidade Federal de Vicosa, Brazil.
Prof. Helena Janols, Infektionsklinien, Skanes Universitetsisjukhus, Sweden.
Prof. Donald R.Barnard, USDA, Agricultural Research Service, CMAVE, USA.
Dr. Keith White, Faculty of Life Science, University of Manchester, UK.
Prof. Marten J.Edwards, Biology Department, Muhlenberg College, USA.
Prof. E. Warchalowska-Sliwa, Polish Academy of Sciences, Poland.
Dr. K. Balakrishnan, Department of Immunology, Madurai Kamaraj University, India.
Dr. J.Joe Hull, USAD-ARS, Arid Land Agricultural Research Centre, USA.
Dr. Neil Audsley, The Food & Environment Research Agency, UK.
Dr. Raman Chandrasekar, Kansas State University, USA.
Dr. B.K. Tyagi, Centre for Research in Medical Entomology (ICMR), Madurai, TN, India.
Prof. Zhongzheng Gui, Sericulture Research Institute, Chinese Academy of Agricultural Sci., China.
Dr. Fang Zhu, Irrigated Agril. Research and Extension Center, Washington State University, USA.
Prof. K. Murugan, Department of Zoology, Bharathiar University, Coimbatore, India.
Dr. Xiao-Wei Wang, Institute of Insect Science, Zhejiang University, China.
Dr. Haijun Xu, Institute of Insect Science, Zhejiang University, China.
Dr. Alisha Anderson, CSIRO Ecosystem Sciences, Australia.
Prof. Eric D.Dodds, Department of Chemistry, University of Nebraska-Lincoln, USA.
Prof. P. Mosae Selvakumar, Department of Chemistry, Karnaya University, Coimbatore, India.
Prof. A.K.Dikshit, Indian Agriculture Research Institute, New Delhi.
Prof. K.R.S. Sambasiva Rao, Dept. of Biotech. & Zoology, Acharya Nagarjuna University, India
Dr. R. Rangeshwaran, National Bureau of Agriculturally Important Insects, Banglore, India.
Dr. V. Selvanarayanan, Faculty of Agriculture, Annamalai University, Tamil Nadu, India.
Prof. Fernando G. Noriega, Florida International University, Miami, USA.
Prof. Ada Rafaeli, Department of Food Quality and Safety, A.R.O., Israel.
Prof. Daphne Q.-D. Pham, Dept. of Biological Sciences, University of Wisconsin-Parkside, USA.
Prof. Emmanuelle Jacquin-Joly, INRA, UMR 1272 Physiologie de lInsecte, Versailles, France.
Prof. Manickam Sugumaran, University of Massachusetts Boston, USA.
Prof. Nannan Liu, Auburn University, USA.
Prof. Michihiro Kobyashi, Nagoya University, Japan.
Prof. Enoch Y.Park, Innovative Joint Research Center, Shizuoka University, Japan.
Prof. Luiz Paulo Moura ANDRIOLI, Universidade de So Paulo, SP - Brazil
Prof. SHIMADA Toru, The University of Tokyo, Japan.
Prof. Erjun Ling, Institute of Plant Physiology and Ecology, China.

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Acknowledgements
Writing and publishing a book requires the assistance of individuals who are
creative, talented, and hard-working. All of these qualities were present in the
individuals assembled to produce this book volume. I would like to express my
heartfelt gratitude to my former teacher Prof. Seo Sook Jae, (GSNU, South Korea),
Prof. Subba Reddy Palli (University of Kentucky, USA), and other external mentors
Prof. Marian R. Goldsmith (University of Rhode Island, USA), Prof. Enoch Y. Park
(Shizuoka University, Japan), Prof. M. Kobayashi (Nagoya University, Japan), Prof.
CHU Jang Hann (National University of Singapore, Singapore), Prof. Thomas W.
Sappington (USDA-ARS, USA), Prof. Fernando G. Noriega (Florida International
University, USA), Dr. Srinivasan Ramasamy, AVRDC, The World Vegetable
Center, Taiwan), Dr. H.C. Sharam (ICRISAT, India), who inspiration and
supported me at many ways for the commencement of this International Book
Mission Program. The book mission program was initiated on May 2010,
completed on March 2014 and published on October 2014. I have no words to
express my feeling for all those who provided valuable contributions from USA,
South Korea, Japan, China, India, Thailand, Taiwan, Bulgaria, France, Iseral, and
Portugal (Contributors name list, see page no. v) and made the completion of this
book possible. We express our appreciation to the following people (Reviewer
name list, see page no. vii) who reviewed various part of the manuscript as it was
being developed and improved quality of each chapter. I thank the ICMR, New
Delhi, and Chinese Academy of Agricultural, China, and Kansas State University for
support from several aspects. Many others (scientists and publishers) have also
allowed us to use their materials in the various chapters, their color image have then
been converted to gray color/BW. Iam especially indebted to International Book
Mission Organization, Academic Publishing Services for the production of book. I
thank my Co-Editors for their continuous vigilance over the book project and for
always giving advance notice of the editing and proofreading schedules. I thank also
my Brintha, P.G., (my wife), who in all possible way, encouragement helped
transform our original efforts into an acceptable final form. I apologize to those
whose work could not be cited owing to space considerations limitation. Further, I
wish to recognize the moral support extended by colleagues and friends. I hope that
this volume will inspire interest on the diverse aspects of insect biochemistry and
molecular biology in aspiring and established scientists.
Raman Chandrasekar

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A Note from the Publisher

Dear Readers,
This edition represents the first number of the Short Views on Insect
Biochemistry and Molecular Biology book series published by International
Book Mission. It serves to show the public how important entomology field in
expanding basic knowledge or in the development of new technologies nowadays,
in virtually all fields of knowledge. We called for piece of work falling into two
volumes (Basic and Advance aspects).
Far from being complete, the 30 chapters clearly structured and simply explained
experts contributions may provide an overview about current and prominent
advances in insect biochemistry and molecular biology which will help students and
researchers to broaden their knowledge and to gain an understanding of both the
challenges and the opportunities behind each approach.
We look forward to receiving new proposals for the new edition 2015 - 2017.
International Book Mission
Academic Publisher
Manager

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