Two novel proteins expressed by the venom glands of Apis mellifera and Nasonia vitripennis share an ancient C1q-like domain
- PMID: 20167013
- DOI: 10.1111/j.1365-2583.2009.00913.x
Two novel proteins expressed by the venom glands of Apis mellifera and Nasonia vitripennis share an ancient C1q-like domain
Abstract
An in-depth proteomic study of previously unidentified two-dimensional polyacrylamide gel electrophoresis spots of honey bee (Apis mellifera, Hymenoptera) venom revealed a new protein with a C1q conserved domain (C1q-VP). BlastP searching revealed a strong identity with only two proteins from other insect species: the jewel wasp, Nasonia vitripennis (Hymenoptera), and the green pea aphid, Acyrthosiphon pisum (Hemiptera). In higher organisms, C1q is the first subcomponent of the classical complement pathway and constitutes a major link between innate and acquired immunity. Expression of C1q-VP in a variety of tissues of honey bee workers and drones was demonstrated. In addition, a wide spatial and temporal pattern of expression was observed in N. vitripennis. We suggest that C1q-VP represents a new member of the emerging group of venom trace elements. Using degenerate primers the corresponding gene was found to be highly conserved in eight hymenopteran species, including species of the Aculeata and the Parasitica groups (suborder Apocrita) and even the suborder Symphyta. A preliminary test using recombinant proteins failed to demonstrate Am_C1q-VP-specific immunoglobulin E recognition by serum from patients with a documented severe bee venom allergy.
Similar articles
-
The insect chemoreceptor superfamily of the parasitoid jewel wasp Nasonia vitripennis.Insect Mol Biol. 2010 Feb;19 Suppl 1:121-36. doi: 10.1111/j.1365-2583.2009.00979.x. Insect Mol Biol. 2010. PMID: 20167023
-
Organization, evolution and transcriptional profile of hexamerin genes of the parasitic wasp Nasonia vitripennis (Hymenoptera: Pteromalidae).Insect Mol Biol. 2010 Feb;19 Suppl 1:137-46. doi: 10.1111/j.1365-2583.2009.00970.x. Insect Mol Biol. 2010. PMID: 20167024
-
Genomics and peptidomics of neuropeptides and protein hormones present in the parasitic wasp Nasonia vitripennis.J Proteome Res. 2010 Oct 1;9(10):5296-310. doi: 10.1021/pr100570j. J Proteome Res. 2010. PMID: 20695486
-
The C1q domain containing proteins: Where do they come from and what do they do?Dev Comp Immunol. 2010 Aug;34(8):785-90. doi: 10.1016/j.dci.2010.02.014. Epub 2010 Mar 16. Dev Comp Immunol. 2010. PMID: 20214925 Review.
-
Bee, wasp and ant venomics pave the way for a component-resolved diagnosis of sting allergy.J Proteomics. 2009 Mar 6;72(2):145-54. doi: 10.1016/j.jprot.2009.01.017. Epub 2009 Jan 21. J Proteomics. 2009. PMID: 19344653 Review.
Cited by
-
Clinical complications in envenoming by Apis honeybee stings: insights into mechanisms, diagnosis, and pharmacological interventions.Front Immunol. 2024 Sep 18;15:1437413. doi: 10.3389/fimmu.2024.1437413. eCollection 2024. Front Immunol. 2024. PMID: 39359723 Free PMC article. Review.
-
An integrated transcriptomic and proteomic approach to identify the main Torymus sinensis venom components.Sci Rep. 2021 Mar 3;11(1):5032. doi: 10.1038/s41598-021-84385-5. Sci Rep. 2021. PMID: 33658582 Free PMC article.
-
Transcriptional Profiles of Diploid Mutant Apis mellifera Embryos after Knockout of csd by CRISPR/Cas9.Insects. 2021 Aug 6;12(8):704. doi: 10.3390/insects12080704. Insects. 2021. PMID: 34442270 Free PMC article.
-
Insights into the venom composition of the ectoparasitoid wasp Nasonia vitripennis from bioinformatic and proteomic studies.Insect Mol Biol. 2010 Feb;19 Suppl 1(Suppl 1):11-26. doi: 10.1111/j.1365-2583.2009.00914.x. Insect Mol Biol. 2010. PMID: 20167014 Free PMC article.
-
Characterization of neutral lipase BT-1 isolated from the labial gland of Bombus terrestris males.PLoS One. 2013 Nov 8;8(11):e80066. doi: 10.1371/journal.pone.0080066. eCollection 2013. PLoS One. 2013. PMID: 24260337 Free PMC article.
MeSH terms
Substances
LinkOut - more resources
Full Text Sources