Insights into the venom composition of the ectoparasitoid wasp <i>Nasonia vitripennis</i> from bioinformatic and proteomic studies

Graaf, Dirk C. de; Aerts, Maarten; Brunain, Marleen; Desjardins, CA; Jacobs, Franciscus; Werren, J. H.; Devreese, Bart

doi:10.1111/j.1365-2583.2009.00914.x

Cited by 179 publications

(247 citation statements)

References 100 publications

Supporting

Mentioning

241

Contrasting

Unclassified

Order By: Relevance

“…Previous studies have demonstrated that arthropod venoms also contain serine protease inhibitors (Yuan et al, 2008;Choo et al, 2012). The expression pattern of Bt-CI in B. terrestris observed here suggests that Bt-CI likely functions as a serine protease inhibitor in the fat body and venom (de Graaf et al, 2010). The venom duct and reservoir in honeybees are characterized by an epicuticular lining (Bridges and Owen, 2005) and endocuticular proteins in the gland tissues (Peiren et al, 2008).…”

Section: Resultssupporting

confidence: 51%

Molecular Cloning and Characterization of Chymotrypsin Inhibitor and Chitin-Binding Protein Homologs from the Bumblebee Bombus terrestris

Qiu¹,

Yoon²,

Jin³

2012

International Journal of Industrial Entomology

View full text Add to dashboard Cite

The bumblebee Bombus terrestris is widely used in greenhouses to pollinate crops. Here, we report the molecular cloning and characterization of chymotrypsin inhibitor and chitin-binding protein homologs from B. terrestris. Two cDNAs encoding chymotrypsin inhibitor (Bt-CI) and chitin-binding protein (Bt-CBP) homologs were cloned from B. terrestris. Gene sequence analysis showed that Bt-CI gene consists of three exons encoding 75 amino acids, including a predicted 20-amino acid signal peptide, while Bt-CBP consists of two exons encoding 78 amino acids, including a predicted 26-amino acid signal peptide. The mature Bt-CI and Bt-CBP peptides contain ten and six conserved cysteine residues, respectively. Database searches using the deduced sequences of Bt-CI and Bt-CBP showed similarity to those from B. impatiens (96% peptide sequence identities). Bt-CI and Bt-CBP were expressed in both the venom gland and fat body of B. terrestris worker bees. The recombinant Bt-CI and Bt-CBP peptides were expressed in baculovirusinfected insect cells. Taken together, our findings describe the molecular characterization of Bt-CI and Bt-CBP from B. terrestris.

show abstract

Section: Resultssupporting

confidence: 51%

Molecular Cloning and Characterization of Chymotrypsin Inhibitor and Chitin-Binding Protein Homologs from the Bumblebee Bombus terrestris

Qiu¹,

Yoon²,

Jin³

2012

International Journal of Industrial Entomology

View full text Add to dashboard Cite

show abstract

“…Wasp venom genes were proposed to encode small, classically secreted proteins (47), and this idea appears to be somewhat true of G1 venom proteins; 28% contained a predicted secretion signal, and these proteins had an average size of 44 kDa. However, venom SERCA is a large (110-kDa) transmembrane protein with no classical secretion signal sequence, and this finding was not unusual across G1 and other Hymenopteran venoms; G1 venom proteins range in size from 9 kDa to 379 kDa, and bioinformatic analyses using transmembrane domain prediction software (48) reveals that 7% (12/166) of G1 venom proteins and 20% (176/864) of the previously identified Hymenopteran venoms in GenBank (30) contain predicted transmembrane domains.…”

Section: Resultsmentioning

confidence: 99%

Parasitoid wasp venom SERCA regulates Drosophila calcium levels and inhibits cellular immunity

Mortimer¹,

Goecks

Kacsoh³

et al. 2013

Proc. Natl. Acad. Sci. U.S.A.

124

View full text Add to dashboard Cite

Because parasite virulence factors target host immune responses, identification and functional characterization of these factors can provide insight into poorly understood host immune mechanisms. The fruit fly Drosophila melanogaster is a model system for understanding humoral innate immunity, but Drosophila cellular innate immune responses remain incompletely characterized. Fruit flies are regularly infected by parasitoid wasps in nature and, following infection, flies mount a cellular immune response culminating in the cellular encapsulation of the wasp egg. The mechanistic basis of this response is largely unknown, but wasps use a mixture of virulence proteins derived from the venom gland to suppress cellular encapsulation. To gain insight into the mechanisms underlying wasp virulence and fly cellular immunity, we used a joint transcriptomic/ proteomic approach to identify venom genes from Ganaspis sp.1 (G1), a previously uncharacterized Drosophila parasitoid species, and found that G1 venom contains a highly abundant sarco/endoplasmic reticulum calcium ATPase (SERCA) pump. Accordingly, we found that fly immune cells termed plasmatocytes normally undergo a cytoplasmic calcium burst following infection, and that this calcium burst is required for activation of the cellular immune response. We further found that the plasmatocyte calcium burst is suppressed by G1 venom in a SERCA-dependent manner, leading to the failure of plasmatocytes to become activated and migrate toward G1 eggs. Finally, by genetically manipulating plasmatocyte calcium levels, we were able to alter fly immune success against G1 and other parasitoid species. Our characterization of parasitoid wasp venom proteins led us to identify plasmatocyte cytoplasmic calcium bursts as an important aspect of fly cellular immunity.

show abstract

“…4). This type of protein is also found in the venom of several parasitoids (de Graaf et al, 2010) and CiBV protein 97b might thus also be a virulence factor. CiBV protein 13c has similarity to S-phase kinaseassociated protein 1A and its transcript increased approximately 20-fold in female pupae (Table 2, Fig.…”

Section: Cibv Gene Products With No Similarity To Viral Proteinsmentioning

confidence: 99%

Identification of bracovirus particle proteins and analysis of their transcript levels at the stage of virion formation

Wetterwald

Roth

Kaeslin

et al. 2010

Journal of General Virology

View full text Add to dashboard Cite

Polydnaviruses (PDVs) are unique symbiotic viruses associated with parasitic wasps; they replicate only in the calyx cells of a wasp's ovaries and are transferred at oviposition along with the parasitoid egg into the lepidopteran host. The DNA packaged in the viral particles encodes factors that manipulate the host's immune defences and development to benefit the parasitoid. PDVs are found in two subfamilies of ichneumonids (ichnoviruses) and in braconids of the microgastroid complex (bracoviruses). We recently showed that the latter derive from an ancestral nudivirus, as 24 nudivirus-related genes were identified in ovaries of two distantly related braconids at the stage of virion formation. Here, we present a comprehensive analysis of the viral particle proteins of the Chelonus inanitus bracovirus (CiBV). Proteins of purified CiBV particles were analysed by mass spectrometry and amino acid sequences matched to the existing ovarian-cDNA database. In addition, transcript quantities of identified genes were measured by quantitative real-time PCR in female pupae at the onset and peak of virion formation and at corresponding stages in male pupae. This combined approach allowed the identification of 44 CiBV particle proteins: 16 were nudivirus-related, three had similarity to ovarian proteins of another braconid, 11 had similarity to cellular proteins and 14 had no similarity to known proteins. The transcripts of all of them increased in female, but not male, pupae. These data confirm the important contribution of nudivirus genes but also indicate the presence of many lineage-or species-specific proteins possibly involved in the parasitoid-host interaction.

show abstract

Insights into the venom composition of the ectoparasitoid wasp Nasonia vitripennis from bioinformatic and proteomic studies

Cited by 179 publications

References 100 publications

Molecular Cloning and Characterization of Chymotrypsin Inhibitor and Chitin-Binding Protein Homologs from the Bumblebee Bombus terrestris

Molecular Cloning and Characterization of Chymotrypsin Inhibitor and Chitin-Binding Protein Homologs from the Bumblebee Bombus terrestris

Parasitoid wasp venom SERCA regulates Drosophila calcium levels and inhibits cellular immunity

Identification of bracovirus particle proteins and analysis of their transcript levels at the stage of virion formation

Contact Info

Product

Resources

About