Cathepsins of lepidopteran insects: Aspects and prospects

Saikhedkar, Nidhi; Summanwar, Aarohi; Joshi, Rakesh S.; Giri, Ashok P.

doi:10.1016/j.ibmb.2015.07.005

Cited by 45 publications

(34 citation statements)

References 65 publications

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“…Homologs of the Cathepsin D family of proteins, which have been implicated in growth, defense and digestion (Saikhedkar et al, 2015; Ahn and Zhu-Salzman, 2009), were present in the TF of both Camponotus species. Prophenoloxidase 2, an enzyme responsible for the melanization involved in the insect immune response (Söderhäll and Cerenius, 1998), was found in the TF of A. mellifera and S. invicta .…”

Section: Discussionmentioning

confidence: 99%

Oral transfer of chemical cues, growth proteins and hormones in social insects

LeBoeuf

Waridel

Brent

et al. 2016

eLife

112

123

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Social insects frequently engage in oral fluid exchange – trophallaxis – between adults, and between adults and larvae. Although trophallaxis is widely considered a food-sharing mechanism, we hypothesized that endogenous components of this fluid might underlie a novel means of chemical communication between colony members. Through protein and small-molecule mass spectrometry and RNA sequencing, we found that trophallactic fluid in the ant Camponotus floridanus contains a set of specific digestion- and non-digestion related proteins, as well as hydrocarbons, microRNAs, and a key developmental regulator, juvenile hormone. When C. floridanus workers’ food was supplemented with this hormone, the larvae they reared via trophallaxis were twice as likely to complete metamorphosis and became larger workers. Comparison of trophallactic fluid proteins across social insect species revealed that many are regulators of growth, development and behavioral maturation. These results suggest that trophallaxis plays previously unsuspected roles in communication and enables communal control of colony phenotypes.DOI: http://dx.doi.org/10.7554/eLife.20375.001

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Section: Discussionmentioning

confidence: 99%

Oral transfer of chemical cues, growth proteins and hormones in social insects

LeBoeuf

Waridel

Brent

et al. 2016

eLife

112

123

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“…There may be applications in managing pests that have overcome resistant cultivars of crops, as resistance to crops (host plants) shares many similarities with insecticide resistance. Some studies have considered the potential for the use of proteases as pest control targets . A group of proteases that could provide a target in the area of pest management are the cathepsins, cysteine/aspartate proteases, especially in Lepidoptera .…”

Section: Opportunities For Management Strategies Using Intracellular mentioning

confidence: 99%

“…These cellular enzymes are involved in processes such as proteostasis, development, growth, metamorphosis, apoptosis and immunity, regulated by activation, inhibition, degradation etc. Stress from virus attack, starvation, host plant defences, temperature and oxidative factors lead to their overexpression; thus this class of proteases are promising candidates as targets . In researching the genetic background in control with pesticides of the beetle Monochamus alternates (main vector in China of the pine wilt disease), cathepsin B, cysteine peptidases, neuropeptides and serine peptidases were found to be important in growth, reproduction behaviour and other physiological processes .…”

Section: Opportunities For Management Strategies Using Intracellular mentioning

confidence: 99%

“…56 A group of proteases that could provide a target in the area of pest management are the cathepsins, cysteine/aspartate proteases, especially in Lepidoptera. 56 These cellular enzymes are involved in processes such as proteostasis, wileyonlinelibrary.com/journal/ps development, growth, metamorphosis, apoptosis and immunity, regulated by activation, inhibition, degradation etc. Stress from virus attack, starvation, host plant defences, temperature and oxidative factors lead to their overexpression; thus this class of proteases are promising candidates as targets.…”

Section: Intracellular Proteases As Targets 521 Enzyme Inhibitorsmentioning

confidence: 99%

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Insecticide resistance and intracellular proteases

Wilkins

2017

Pest Management Science

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Pesticide resistance is an example of evolution in action with mechanisms of resistance arising from mutations or increased expression of intrinsic genes. Intracellular proteases have a key role in maintaining healthy cells and in responding to stressors such as pesticides. Insecticide-resistant insects have constitutively elevated intracellular protease activity compared to corresponding susceptible strains. This increase was shown for some cases originally through biochemical enzyme studies and subsequently putatively by transcriptomics and proteomics methods. Upregulation and expression of proteases have been characterised in resistant strains of some insect species, including mosquitoes. This increase in proteolysis results in more degradation products (amino acids) of intracellular proteins. These may be utilised in the resistant strain to better protect the cell from stress. There are changes in insect intracellular proteases shortly after insecticide exposure, suggesting a role in stress response. The use of protease and proteasome inhibitors or peptide mimetics as synergists with improved application techniques and through protease gene knockdown using RNA interference (possibly expressed in crop plants) may be potential pest management strategies, in situations where elevated intracellular proteases are relevant. © 2017 Society of Chemical Industry.

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“…Ji et al (2017) report that silencing of endo-β-1,4-glucanase in the saliva of N. lugens decreases its capacity to feed and reproduce on rice plants (Ji et al, 2017). Cysteine proteases such as cathepsins are important cellular enzymes involved in insect growth and development (Saikhedkar et al, 2015). NAMLAA cleaves the link between l-amino acid residues and N-acetylmuramoyl in specific cell-wall glycopeptides (Wang et al, 2003).…”

Section: Enzymesmentioning

confidence: 99%

The secreted salivary proteome of Asian citrus psyllid Diaphorina citri

Killiny

2018

Physiol. Entomol.

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The Asian citrus psyllid Diaphorina citri Kuwayama is a sap‐sucking hemipteran that serves as a vector for Candidatus Liberibacter asiaticus (CLas), the causal agent of citrus huanglongbing (HLB). Salivary secretions play critical roles in insect–host plant interactions and are responsible for the establishment of insect herbivory. In the present study, we aim to identify the major proteins in D. citri saliva. Saliva proteins are collected from the artificial diet upon D. citri feeding. Collected proteins are concentrated, filtered, digested and then analyzed using liquid chromatography‐tandem spectrometry (MS/MS). The MS/MS data are then analyzed by searching the D. citri genome deposited in the NCBI. Eighty‐nine proteins are identified in D. citri saliva. Eighty‐six of these proteins are from D. citri, whereas three proteins are from Wolbachia endosymbiont. The proteins identified belong to several functional groups, including enzymes, cytoskeletal proteins, sheath proteins, receptor proteins, transporter proteins, chromatin‐, RNA‐ and DNA‐binding proteins, and other proteins. These proteins could be involved in many key functions, including detoxification of plant defencee compounds and suppression of plant defence, as well as facilitation of stylet penetration, sap sucking and digestion. The identification of these proteins is an essential step for the understanding of D. citri–plant interactions. The identification of key enzymes in the saliva of D. citri could lead to a discovery of proper inhibitors that disrupt its feeding, consequently preventing the spread of the HLB pathogen.

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Cathepsins of lepidopteran insects: Aspects and prospects

Cited by 45 publications

References 65 publications

Oral transfer of chemical cues, growth proteins and hormones in social insects

Oral transfer of chemical cues, growth proteins and hormones in social insects

Insecticide resistance and intracellular proteases

The secreted salivary proteome of Asian citrus psyllid Diaphorina citri

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