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两种新型蛋白由蜜蜂和丽蝇毒腺表达,它们共享一个古老的 C1q 样结构域。

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

机构信息

Laboratory of Zoophysiology, Ghent University, Ghent, Belgium.

出版信息

Insect Mol Biol. 2010 Feb;19 Suppl 1:1-10. doi: 10.1111/j.1365-2583.2009.00913.x.


DOI:10.1111/j.1365-2583.2009.00913.x
PMID:20167013
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.

摘要

对先前未鉴定的蜜蜂(Apis mellifera,膜翅目)毒液二维聚丙烯酰胺凝胶电泳点的深入蛋白质组学研究揭示了一种具有 C1q 保守结构域(C1q-VP)的新蛋白质。BlastP 搜索仅显示与来自其他昆虫物种的两种蛋白质具有很强的同一性:宝石黄蜂(Nasonia vitripennis,膜翅目)和绿豆蚜(Acyrthosiphon pisum,半翅目)。在高等生物中,C1q 是经典补体途径的第一个亚基,是先天免疫和获得性免疫之间的主要联系。证明 C1q-VP 在工蜂和雄蜂的多种组织中表达。此外,在 N. vitripennis 中观察到广泛的时空表达模式。我们认为 C1q-VP 代表新兴的毒液痕量元素组的一个新成员。使用简并引物发现相应的基因在包括 Aculeata 和 Parasitica 组(亚目 Apocrita)甚至 Symphyta 的 8 种膜翅目物种中高度保守。使用重组蛋白进行的初步测试未能证明 Am_C1q-VP 特异性免疫球蛋白 E 由具有记录的严重蜂毒液过敏的患者的血清识别。

相似文献

[1]
Two novel proteins expressed by the venom glands of Apis mellifera and Nasonia vitripennis share an ancient C1q-like domain.

Insect Mol Biol. 2010-2

[2]
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[3]
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[4]
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[5]
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Insect Mol Biol. 2013-1-25

[6]
[Cloning and comparative analysis of the venom prepromelittin genes from four wasp species].

Yi Chuan Xue Bao. 2003-6

[7]
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Arch Insect Biochem Physiol. 2002-8

[8]
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[9]
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[10]
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Arch Insect Biochem Physiol. 2009-8

引用本文的文献

[1]
Clinical complications in envenoming by honeybee stings: insights into mechanisms, diagnosis, and pharmacological interventions.

Front Immunol. 2024

[2]
Invertebrate C1q Domain-Containing Proteins: Molecular Structure, Functional Properties and Biomedical Potential.

Mar Drugs. 2023-10-30

[3]
Transcriptional Profiles of Diploid Mutant Embryos after Knockout of by CRISPR/Cas9.

Insects. 2021-8-6

[4]
An integrated transcriptomic and proteomic approach to identify the main Torymus sinensis venom components.

Sci Rep. 2021-3-3

[5]
Spermatogenesis in haploid males of the jewel wasp Nasonia vitripennis.

Sci Rep. 2019-8-21

[6]
Venom gland components of the ectoparasitoid wasp, Anisopteromalus calandrae.

J Venom Res. 2015-12-24

[7]
Hymenoptera allergens: from venom to "venome".

Front Immunol. 2014-2-28

[8]
Characterization of neutral lipase BT-1 isolated from the labial gland of Bombus terrestris males.

PLoS One. 2013-11-8

[9]
Venom proteins of the parasitoid wasp Nasonia vitripennis: recent discovery of an untapped pharmacopee.

Toxins (Basel). 2010-3-30

[10]
Insights into the venom composition of the ectoparasitoid wasp Nasonia vitripennis from bioinformatic and proteomic studies.

Insect Mol Biol. 2010-2

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