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Two novel proteins expressed by the venom glands of Apis mellifera and Nasonia vitripennis share an ancient C1q‐like domain
Author(s) -
De Graaf D. C.,
Brunain M.,
Scharlaken B.,
Peiren N.,
Devreese B.,
Ebo D. G.,
Stevens W. J.,
Desjardins C. A.,
Werren J. H.,
Jacobs F. J.
Publication year - 2010
Publication title -
insect molecular biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.955
H-Index - 93
eISSN - 1365-2583
pISSN - 0962-1075
DOI - 10.1111/j.1365-2583.2009.00913.x
Subject(s) - nasonia vitripennis , acyrthosiphon pisum , biology , hymenoptera , venom , honey bee , aphid , botany , zoology , biochemistry , aphididae , pest analysis , pteromalidae , homoptera , parasitoid
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). B last P 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.