通过AAT三联体重复在人类免疫缺陷病毒1型表面糖蛋白可变区插入N-连接糖基化位点。
Insertion of N-linked glycosylation sites in the variable regions of the human immunodeficiency virus type 1 surface glycoprotein through AAT triplet reiteration.
作者信息
Bosch M L, Andeweg A C, Schipper R, Kenter M
机构信息
Laboratory of Immunobiology, National Institute for Public Health and Environmental Protection, The Netherlands.
出版信息
J Virol. 1994 Nov;68(11):7566-9. doi: 10.1128/JVI.68.11.7566-7569.1994.
Abstract
Variable regions with sequence length variation in the human immunodeficiency virus type 1 envelope exhibit an unusual pattern of codon usage with AAT, ACT, and AGT together composing > 70% of all codons used. We postulate that this distribution is caused by insertion of AAT triplets followed by point mutations and selection. Accumulation of the encoded amino acids (asparagine, serine, and threonine) leads to the creation of new N-linked glycosylation sites, which helps the virus to escape from the immune pressure exerted by virus-neutralizing antibodies.
摘要
人类免疫缺陷病毒1型包膜中具有序列长度变异的可变区呈现出一种不寻常的密码子使用模式，其中AAT、ACT和AGT共同构成了所有使用密码子的70%以上。我们推测这种分布是由AAT三联体的插入，随后是点突变和选择导致的。编码氨基酸（天冬酰胺、丝氨酸和苏氨酸）的积累导致新的N-连接糖基化位点的产生，这有助于病毒逃避病毒中和抗体施加的免疫压力。
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