Rapid expansion of the protein disulfide isomerase gene family facilitates the folding of venom peptides

Safavi-­Hemami, Helena; Li, Qing; Jackson, Ronneshia L.; Song, Albert S.; Boomsma, Wouter; Bandyopadhyay, Pradip K.; Gruber, Christian W.; Purcell, Anthony W.; Yandell, Mark; Olivera, Baldomero M.; Ellgaard, Lars

doi:10.1073/pnas.1525790113

Cited by 45 publications

(52 citation statements)

References 34 publications

(35 reference statements)

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“…Interestingly, the rapid expansion of a large gene family encoding PDIs specifically-expressed in the venom glands of cone snails has been recently suggested to facilitate the folding of the numerous conotoxins produced by these marine predators32. Here, however, phylogenetic analysis shows that Psyttalia venomous PDI sequences group with different PDIs from braconid wasps (Supplementary Figure S6), suggesting that no specific expansion occurred.…”

Section: Resultsmentioning

confidence: 82%

Comparative venomics of Psyttalia lounsburyi and P. concolor, two olive fruit fly parasitoids: a hypothetical role for a GH1 β-glucosidase

Mathe‐Hubert

Colinet

Deleury

et al. 2016

Sci Rep

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Venom composition of parasitoid wasps attracts increasing interest – notably molecules ensuring parasitism success on arthropod pests – but its variation within and among taxa is not yet understood. We have identified here the main venom proteins of two braconid wasps, Psyttalia lounsburyi (two strains from South Africa and Kenya) and P. concolor, olive fruit fly parasitoids that differ in host range. Among the shared abundant proteins, we found a GH1 β-glucosidase and a family of leucine-rich repeat (LRR) proteins. Olive is extremely rich in glycoside compounds that are hydrolyzed by β-glucosidases into defensive toxic products in response to phytophagous insect attacks. Assuming that Psyttalia host larvae sequester ingested glycosides, the injected venom GH1 β-glucosidase could induce the release of toxic compounds, thus participating in parasitism success by weakening the host. Venom LRR proteins are similar to truncated Toll-like receptors and may possibly scavenge the host immunity. The abundance of one of these LRR proteins in the venom of only one of the two P. lounsburyi strains evidences intraspecific variation in venom composition. Altogether, venom intra- and inter-specific variation in Psyttalia spp. were much lower than previously reported in the Leptopilina genus (Figitidae), suggesting it might depend upon the parasitoid taxa.

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Section: Resultsmentioning

confidence: 82%

Comparative venomics of Psyttalia lounsburyi and P. concolor, two olive fruit fly parasitoids: a hypothetical role for a GH1 β-glucosidase

Mathe‐Hubert

Colinet

Deleury

et al. 2016

Sci Rep

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“…PDIs are involved in the folding of proteins by catalysing the oxidation, isomerization and reduction of disulfide bonds, that covalently link specific cysteine residues and confer stability to proteins [113,114]. In venomous cone snails, PDIs are strictly localized in the venom glands, where they guide the folding of cysteine-rich peptide toxins (conotoxins) into their native state, while they are absent in the secreted venom [115,116]. Indeed, PDIs are mainly localized in the endoplasmic reticulum, and their presence in the extracellular space is considered rather rare [117].…”

Section: Discussionmentioning

confidence: 99%

Venomics of the ectoparasitoid wasp Bracon nigricans

Becchimanzi¹,

Avolio²,

Bostan³

et al. 2020

BMC Genomics

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Background: Venom is one of the most important sources of regulation factors used by parasitic Hymenoptera to redirect host physiology in favour of the developing offspring. This has stimulated a number of studies, both at functional and "omics" level, which, however, are still quite limited for ectophagous parasitoids that permanently paralyze and suppress their victims (i.e., idiobiont parasitoids). Results: Here we present a combined transcriptomic and proteomic study of the venom of the generalist idiobiont wasp Bracon nigricans, an ectophagous larval parasitoid of different lepidopteran species, for which we recently described the host regulation strategy and the functional role of the venom in the induction of physiological changes in parasitized hosts. The experimental approach used led to the identification of the main components of B. nigricans venom involved in host regulation. Enzymes degrading lipids, proteins and carbohydrates are likely involved in the mobilization of storage nutrients from the fat body and may concurrently be responsible for the release of neurotoxic fatty acids inducing paralysis, and for the modulation of host immune responses. Conclusion:The present work contributes to fill the gap of knowledge on venom composition in ectoparasitoid wasps, and, along with our previous physiological study on this species, provides the foundation on which to develop a functional model of host regulation, based both on physiological and molecular data. This paves the way towards a better understanding of parasitism evolution in the basal lineages of Hymenoptera and to the possible exploitation of venom as source of bioinsecticidal molecules.

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“…The substrate range of PDI in vivo is clearly very wide but it is not limitless. Toxins from marine snails such as cone snails (Conus) comprise a vast diversity of disulfide-bonded proteins which include unique structural domains expressed only in conoidean venoms [40] . This rapid evolution of an unprecedented diversity of disulfide-bonded structural domains has been accompanied by the evolution of a large number of conotoxin-specific PDIs each expressed at high levels within the venom gland.…”

Section: Pdi As Catalyst Of Oxidative Protein Folding In Cementioning

confidence: 99%

‘Something in the way she moves’: The functional significance of flexibility in the multiple roles of protein disulfide isomerase (PDI)

Freedman

Desmond

Byrne

et al. 2017

Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics

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Protein disulfide isomerase (PDI) has diverse functions in the endoplasmic reticulum as catalyst of redox transfer, disulfide isomerization and oxidative protein folding, as molecular chaperone and in multi-subunit complexes. It interacts with an extraordinarily wide range of substrate and partner proteins, but there is only limited structural information on these interactions. Extensive evidence on the flexibility of PDI in solution is not matched by any detailed picture of the scope of its motion. A new rapid method for simulating the motion of large proteins provides detailed molecular trajectories for PDI demonstrating extensive changes in the relative orientation of its four domains, great variation in the distances between key sites and internal motion within the core ligand-binding domain. The review shows that these simulations are consistent with experimental evidence and provide insight into the functional capabilities conferred by the extensive flexible motion of PDI.

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Rapid expansion of the protein disulfide isomerase gene family facilitates the folding of venom peptides

Cited by 45 publications

References 34 publications

Comparative venomics of Psyttalia lounsburyi and P. concolor, two olive fruit fly parasitoids: a hypothetical role for a GH1 β-glucosidase

Comparative venomics of Psyttalia lounsburyi and P. concolor, two olive fruit fly parasitoids: a hypothetical role for a GH1 β-glucosidase

Venomics of the ectoparasitoid wasp Bracon nigricans

‘Something in the way she moves’: The functional significance of flexibility in the multiple roles of protein disulfide isomerase (PDI)

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