An Ovarian Protein Involved in Passive Avoidance of an Endoparasitoid To Evade Its Host Immune Response

Teng, Ziwen; Wu, Huizi; Ye, Xinhai; Xiong, Shijiao; Xu, Gang; Wang, Fang; Fang, Qi; Yè, Gōngyín

doi:10.1021/acs.jproteome.8b00824

Cited by 15 publications

(26 citation statements)

References 39 publications

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“…In contrast, endoparasitoids oviposit into the host hemocoel (Asgari and Rivers, 2011). To assist successful development of offspring, female wasps inject multiple virulence factors into the host, including venom proteins (Asgari and Rivers, 2011;Moreau and Asgari, 2015;Wan et al, 2019), polydnaviruses (PDVs) (Ye et al, 2018), ovarian fluids (Teng et al, 2019), virus-like particles (VLPs) (Harvey et al, 2013). Venom proteins, an indispensable part of virulence factors, inhibit immunity, interrupt development, and regulate metabolism of the host (Asgari and Rivers, 2011;Moreau and Asgari, 2015).…”

Section: Introductionmentioning

confidence: 99%

“…Venom proteins comprise various bioactive molecules, such as enzymes, protease inhibitors, recognition and binding proteins, and other unknown compounds (Asgari and Rivers, 2011;Moreau and Asgari, 2015). So far, many venom components have been extensively investigated, such as RhoGAP (Labrosse et al, 2005a,b;Colinet et al, 2007), calreticulin (CRT) (Zhang et al, 2006;Wang et al, 2013;Siebert et al, 2015), sarco/endoplasmic reticulum calcium ATPase (SERCA) (Mortimer et al, 2013), GH1 β-glucosidase (Hubert et al, 2016), α-amylases (Wang et al, 2019), Crp32B (Teng et al, 2019). They inhibit host cell spreading, prevent host cellular encapsulation, suppress host hemolymph melanization or hydrolyze nutrients of the host to guarantee survival of wasp progeny.…”

Section: Introductionmentioning

confidence: 99%

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Identification and Comparative Analysis of Venom Proteins in a Pupal Ectoparasitoid, Pachycrepoideus vindemmiae

Yang

Liu

et al. 2020

Front. Physiol.

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Parasitoid wasps inject venom containing complex bioactive compounds to regulate the immune response and development of host arthropods and sometime paralyze host arthropods. Although extensive studies have been conducted on the identification of venom proteins in larval parasitoids, relatively few studies have examined the pupal parasitoids. In our current study, a combination of transcriptomic and proteomic methods was used to identify 64 putative venom proteins from Pachycrepoideus vindemmiae, an ectoparasitoid of Drosophila. Expression analysis revealed that 20 tested venom proteins have 419-fold higher mean expression in the venom apparatus than in other wasp tissues, indicating their specialization to venom. Comparisons of venom proteins from P. vindemmiae and other five species spanning three parasitoid families detected a core set of "ancient" orthologs in Pteromalidae. Thirty-five venom proteins of P. vindemmiae were assigned to the orthologous groups by reciprocal best matches with venoms of other pteromalids, while the remaining 29 were not. Of the 35 categories, twenty-seven have orthologous relationships with Nasonia vitripennis venom proteins and 25 with venoms of Pteromalus puparum. More distant relationships detected that five and two venom proteins of P. vindemmiae are orthologous with venoms of two Figitidae parasitoids and a Braconidae representative, respectively. Moreover, twenty-two venoms unique to P. vindemmiae were also detected, indicating considerable interspecific variation of venom proteins in parasitoids. Phylogenetic reconstruction based on a set of single-copy genes clustered P. vindemmiae with P. puparum, N. vitripennis, and other members of the family Pteromalidae. These findings provide strong evidence that P. vindemmiae venom proteins are well positioned for future functional and evolutionary studies.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Identification and Comparative Analysis of Venom Proteins in a Pupal Ectoparasitoid, Pachycrepoideus vindemmiae

Yang

Liu

et al. 2020

Front. Physiol.

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“…The expression of the identified TnBV genes, that are responsible for morphological alterations and apoptosis in haemocytes, always occurs at least after 3-4 h [24,26]. We hypothesize that the very early suppression of the host immune response after oviposition is correlated to both a passive mechanism, due to the presence of a fibrous layer on the egg surface, and an active mechanism, due to the action of the possible synergic effect of the venom and OP mixture [47][48][49]. The venom composition was elucidated by using a combined transcriptomic and proteomic approach [15] and several proteins putatively involved in the alteration of the immune system of the parasitized host identified.…”

Section: Introductionmentioning

confidence: 96%

Role of Ovarian Proteins Secreted by Toxoneuron nigriceps (Viereck) (Hymenoptera, Braconidae) in the Early Suppression of Host Immune Response

Salvia

Scieuzo

Grimaldi

et al. 2021

Insects

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Toxoneuron nigriceps (Viereck) (Hymenoptera, Braconidae) is an endophagous parasitoid of the larval stages of the tobacco budworm, Heliothis virescens (Fabricius) (Lepidoptera, Noctuidae). During oviposition, T. nigriceps injects into the host body, along with the egg, the venom, the calyx fluid, which contains a Polydnavirus (T. nigriceps BracoVirus: TnBV), and the Ovarian Proteins (OPs). Although viral gene expression in the host reaches detectable levels after a few hours, a precocious disruption of the host metabolism and immune system is observed right after parasitization. This alteration appears to be induced by female secretions including TnBV venom and OPs. OPs, originating from the ovarian calyx cells, are involved in the induction of precocious symptoms in the host immune system alteration. It is known that OPs in braconid and ichneumonid wasps can interfere with the cellular immune response before Polydnavirus infects and expresses its genes in the host tissues. Here we show that T. nigriceps OPs induce several alterations on host haemocytes that trigger cell death. The OP injection induces an extensive oxidative stress and a disorganization of actin cytoskeleton and these alterations can explain the high-level of haemocyte mortality, the loss of haemocyte functionality, and so the reduction in encapsulation ability by the host.

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“…In the typical case, virulence factors are classified into venom proteins (Asgari & Rivers, 2011; Glupov & Kryukova, 2016), polydnaviruses (Gundersen‐Rindal, Dupuy, Huguet, & Drezen, 2013), virus‐like particles (Grgacic & Anderson, 2006), ovarian secretions (Mabiala‐Moundoungou, Doury, Eslin, Cherqui, & Prevost, 2010; Teng et al, 2019) and teratocytes (Wang et al, 2018). The virulence factor types and their roles in host physiological manipulation vary a lot in different host/parasitoid relationships, some or all these factors collaborate with each other to ensure successful parasitism, and among which the venom proteins are thoroughly investigated.…”

Section: Introductionmentioning

confidence: 99%

A venom protein, Kazal‐type serine protease inhibitor, of ectoparasitoid Pachycrepoideus vindemiae inhibits the hemolymph melanization of host Drosophila melanogaster

Yang

Qiu

Fang

et al. 2020

Arch Insect Biochem Physiol

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Parasitic wasps inject various virulence factors into the host insects while laying eggs, among which the venom proteins, one of the key players in host insect/parasitoid relationships, act in host cellular and humoral immune regulation to ensure successful development of wasp progeny. Although the investigations into actions of venom proteins are relatively ample in larval parasitoids, their regulatory mechanisms have not been thoroughly understood in pupal parasitoids. Here, we identified a venom protein, Kazal-type serine protease inhibitor, in the pupal ectoparasitoid Pachycrepoideus vindemiae (PvKazal). Sequence analysis revealed that PvKazal is packed by a signal peptide and a highly conserved "Kazal" domain. Quantitative polymerase chain reaction analysis recorded a higher transcript level of PvKazal in the venom apparatus relative to that in the carcass, and the PvKazal messenger RNA level appeared to reach a peak on day 5 posteclosion. Recombinant PvKazal strongly inhibited the hemolymph melanization of host Drosophila melanogaster. Additionally, the heterologous expression of PvKazal in transgenic Drosophila reduced the crystal cell numbers and blocked the melanization of host pupal hemolymph. Our present work underlying the roles of PvKazal undoubtedly increases the understanding of venom-mediated hostparasitoid crosstalk.

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An Ovarian Protein Involved in Passive Avoidance of an Endoparasitoid To Evade Its Host Immune Response

Cited by 15 publications

References 39 publications

Identification and Comparative Analysis of Venom Proteins in a Pupal Ectoparasitoid, Pachycrepoideus vindemmiae

Identification and Comparative Analysis of Venom Proteins in a Pupal Ectoparasitoid, Pachycrepoideus vindemmiae

Role of Ovarian Proteins Secreted by Toxoneuron nigriceps (Viereck) (Hymenoptera, Braconidae) in the Early Suppression of Host Immune Response

A venom protein, Kazal‐type serine protease inhibitor, of ectoparasitoid Pachycrepoideus vindemiae inhibits the hemolymph melanization of host Drosophila melanogaster

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