Identification and characterization of gp65, a salivary-gland-specific molecule expressed in the malaria vector Anopheles albimanus
Identification and characterization of gp65, a salivary-gland-specific molecule expressed in the malaria vector Anopheles albimanus
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DOI：
10.1111/j.0962-1075.2004.00473.x
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发表时间：
2004-04-01
影响因子：
2.6
通讯作者：
de la Cruz Hernandez-Hernandez, F
中科院分区：
文献类型：
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作者：
Montero-Solis, C;Gonzalez-Ceron, L;de la Cruz Hernandez-Hernandez, F
在白纹按蚊中鉴定出一组唾液腺特异性蛋白，命名为gp 65。二维凝胶电泳将这一组分离为至少四个分子，pI为6.4-6.5。确定主要物种gp 65 -1的N-末端氨基酸序列，并使用简并寡核苷酸引物扩增用于文库筛选的特异性探针。回收了一个1312 bp的cDNA克隆，其编码386个氨基酸的预测翻译产物。gp 65 -1在成年雌性腺体的内侧叶和远侧叶中大量表达，并分泌到唾液中。该氨基酸序列具有N-糖基化、磷酸化和肉豆蔻基化的潜在位点，并且与来自其他蚊子物种的许多未知功能的蛋白质相似。
A group of salivary-gland-specific proteins, designated gp65, were identified in the mosquito Anopheles albimanus. Two-dimensional gel electrophoresis resolved this group into at least four molecules with pI 6.4-6.5. The N-terminal amino acid sequence was determined for the major species, gp65-1, and degenerate oligonucleotide primers were used to amplify a specific probe for library screening. A 1312 bp cDNA clone encoding a predicted translation product of 386 amino acids was recovered. gp65-1 is expressed abundantly in the medial and distal-lateral lobes of the adult female glands, and is secreted in the saliva. The amino acid sequence has potential sites for N-glycosylation, phosphorylation and myristylation, and is similar to a number of proteins of unknown function from other mosquito species.