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Two novel proteins expressed by the venom glands of Apis mellifera and Nasonia vitripennis share an ancient C1q-like domain

(2010) INSECT MOLECULAR BIOLOGY. 19(suppl. 1). p.1-10
Author
Organization
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.
Keywords
Nasonia vitripennis, venom, insect, Hymenoptera, Apis mellifera, HONEYBEE VENOM, STRUCTURAL-CHARACTERIZATION, GLOBULAR DOMAIN, HOST, WASP, BEE, HYMENOPTERA, METABOLISM, FLY

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MLA
de Graaf, Dirk, Marleen Brunain, B Scharlaken, et al. “Two Novel Proteins Expressed by the Venom Glands of Apis Mellifera and Nasonia Vitripennis Share an Ancient C1q-like Domain.” INSECT MOLECULAR BIOLOGY 19.suppl. 1 (2010): 1–10. Print.
APA
de Graaf, Dirk, Brunain, M., Scharlaken, B., Peiren, N., Devreese, B., Ebo, D., Stevens, W., et al. (2010). Two novel proteins expressed by the venom glands of Apis mellifera and Nasonia vitripennis share an ancient C1q-like domain. INSECT MOLECULAR BIOLOGY, 19(suppl. 1), 1–10.
Chicago author-date
de Graaf, Dirk, Marleen Brunain, B Scharlaken, N Peiren, Bart Devreese, DG Ebo, WJ Stevens, CA Desjardins, JH Werren, and Franciscus Jacobs. 2010. “Two Novel Proteins Expressed by the Venom Glands of Apis Mellifera and Nasonia Vitripennis Share an Ancient C1q-like Domain.” Insect Molecular Biology 19 (suppl. 1): 1–10.
Chicago author-date (all authors)
de Graaf, Dirk, Marleen Brunain, B Scharlaken, N Peiren, Bart Devreese, DG Ebo, WJ Stevens, CA Desjardins, JH Werren, and Franciscus Jacobs. 2010. “Two Novel Proteins Expressed by the Venom Glands of Apis Mellifera and Nasonia Vitripennis Share an Ancient C1q-like Domain.” Insect Molecular Biology 19 (suppl. 1): 1–10.
Vancouver
1.
de Graaf D, Brunain M, Scharlaken B, Peiren N, Devreese B, Ebo D, et al. Two novel proteins expressed by the venom glands of Apis mellifera and Nasonia vitripennis share an ancient C1q-like domain. INSECT MOLECULAR BIOLOGY. 2010;19(suppl. 1):1–10.
IEEE
[1]
D. de Graaf et al., “Two novel proteins expressed by the venom glands of Apis mellifera and Nasonia vitripennis share an ancient C1q-like domain,” INSECT MOLECULAR BIOLOGY, vol. 19, no. suppl. 1, pp. 1–10, 2010.
@article{1089753,
  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.}},
  author       = {{de Graaf, Dirk and Brunain, Marleen and Scharlaken, B and Peiren, N and Devreese, Bart and Ebo, DG and Stevens, WJ and Desjardins, CA and Werren, JH and Jacobs, Franciscus}},
  issn         = {{0962-1075}},
  journal      = {{INSECT MOLECULAR BIOLOGY}},
  keywords     = {{Nasonia vitripennis,venom,insect,Hymenoptera,Apis mellifera,HONEYBEE VENOM,STRUCTURAL-CHARACTERIZATION,GLOBULAR DOMAIN,HOST,WASP,BEE,HYMENOPTERA,METABOLISM,FLY}},
  language     = {{eng}},
  number       = {{suppl. 1}},
  pages        = {{1--10}},
  title        = {{Two novel proteins expressed by the venom glands of Apis mellifera and Nasonia vitripennis share an ancient C1q-like domain}},
  url          = {{http://dx.doi.org/10.1111/j.1365-2583.2009.00913.x}},
  volume       = {{19}},
  year         = {{2010}},
}

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