Hosts of the Parasitoid Pachycrepoideus vindemmiae (Rondani) (Hymenoptera: Pteromalidae) of Medical-Veterinary and Economic Importance Collected in the State of Goiás, Brazil

Marchiori, Carlos Henrique

doi:10.11648/j.ajls.20130105.14

Cited by 11 publications

(9 citation statements)

References 4 publications

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“…To date, venom proteins of endoparasitoids are relatively well studied (Labrosse et al, 2005a,b;Colinet et al, 2009;Furihata et al, 2013;Goecks et al, 2013;Heavner et al, 2013;Mortimer et al, 2013). However, the venom protein repertoire of ectoparasitoids is less well known (Marchiori and Barbaresco, 2007;Marchiori et al, 2013;Chen et al, 2015;Marchiori and Borges, 2017).…”

Section: Introductionmentioning

confidence: 99%

“…Pachycrepoideus vindemmiae belongs to the family Pteromalidae (Hymenoptera). It is a versatile and solitary pupal ectoparasitoid that parasitizes various flies, including the genera of Drosophila, Musca, Anastrepha, Calliphora, and so on (Marchiori and Barbaresco, 2007;Marchiori et al, 2013;Marchiori and Borges, 2017). In this study, we examined the diversity of P. vindemmiae venom compositions based on both transcriptome-sequencing and proteome analysis, and compared it to venoms of three parasitoid families.…”

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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“…Pachycrepoideus vindemmiae is considered to be a solitary parasitoid that controls a great number of Diptera in the families Anthomyiidae, Calliphoridae, Muscidae, Sarcophagidae, Tachinidae and Tephritidae. This species presents diversified (cosmopolitan) distribution and it has been found in North America and Africa (Gauld and Bolton 1988, Marchiori and Penteado-Dias 2010, Marchiori 2013a, 2013b, Marchiori et al 2013).…”

Section: Resultsmentioning

confidence: 99%

Natural Enemies of Chrysomya albiceps (Wiedemann) (Diptera: Calliphoridae) Collected in States Goiás and Minas Gerais, Brazil

Marchiori¹

2014

IJB

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Chrysomya albiceps (Wiedemann) (Diptera: Calliphoridae) is of great medical importance because it produces myiasis. It has a significant role as a predator of other dipterous larvae. Moreover, this dipterous insect is of great importance with regard to public health because it mechanically carries pathogens to humans. This study had the objective of ascertaining the species of parasitoids of C. albiceps in human feces, cattle liver, cattle kidney, chicken viscera, fish and pig carcasses in Goiás and Minas Gerais, from October 1999 to November 2013. Pupae were obtained by means of the flotation method. They were individually placed in gelatin capsules until the adult flies or their parasitoids emerged. Nasonia vitripennis (Walker) (Hymenoptera: Pteromalidae) was the most frequent species with a percentage of 42.4%. Pachycrepoideus vindemmiae was the species that showed a highest percentage of parasitism.

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“…As a versatile pupal ectoparasitoid, P. vindemiae, (Pteromalidae: Hymenoptera), has a wide host range [18][19][20][21][22]. Venom proteins are the only virulence factor for successful parasitism by P. vindemiae, and they are responsible for manipulating the host immune system [23].…”

Section: Introductionmentioning

confidence: 99%

Functional Characterization of a Venom Protein Calreticulin in the Ectoparasitoid Pachycrepoideus vindemiae

Yang

Wang

Qiu

et al. 2019

Insects

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Venom proteins act in the immunological interactions between parasitoids and their host insects. The effect of venom proteins on host immunity is not fully understood in pupal parasitoids. We identified the functions of a venom protein, calreticulin (PvCRT), in the pupal ectoparasitoid Pachycrepoideus vindemiae. Here, we report that PvCRT features a signal peptide and two conserved “calreticulin” domains. Multiple sequence alignments show that PvCRT shares 83.54% amino acid identity with CRT from both Pteromalus puparum and Nasonia vitripennis, which infers a close relationship among these three species. Using qPCR analysis, we found a lower expression level of PvCRT (0.27-fold) in the venom apparatus compared to the corresponding carcass. Immunohistochemical localization revealed that PvCRT was ubiquitously expressed in venom gland. The expression of the PvCRT gene in Drosophila transgenic lines via the UAS/Gal4 binary expression system reduced the self-encapsulation phenotype of tu(1)Sz1 mutants. Additionally, studies on humoral immunity indicate that PvCRT does not affect the antimicrobial immune responses of the host. This work on an ectoparasitoid will increase our understanding of venom–mediated host-parasitoid interactions.

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Hosts of the Parasitoid Pachycrepoideus vindemmiae (Rondani) (Hymenoptera: Pteromalidae) of Medical-Veterinary and Economic Importance Collected in the State of Goiás, Brazil

Cited by 11 publications

References 4 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

Natural Enemies of Chrysomya albiceps (Wiedemann) (Diptera: Calliphoridae) Collected in States Goiás and Minas Gerais, Brazil

Functional Characterization of a Venom Protein Calreticulin in the Ectoparasitoid Pachycrepoideus vindemiae

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