Proteolytic Processing of the Human Immunodeficiency Virus Envelope Glycoprotein Precursor Decreases Conformational Flexibility
Proteolytic Processing of the Human Immunodeficiency Virus Envelope Glycoprotein Precursor Decreases Conformational Flexibility
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DOI：
10.1128/jvi.02765-12
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发表时间：
2013-02-01
影响因子：
5.4
通讯作者：
Sodroski, Joseph
中科院分区：
文献类型：
--
作者：
Haim, Hillel;Salas, Ignacio;Sodroski, Joseph
人类免疫缺陷病毒1型(HIV-1)病毒粒子表面的成熟包膜糖蛋白(Env)尖峰是由三聚体gp160糖蛋白前体蛋白裂解而来的。值得注意的是，HIV-1Env前体的蛋白水解性处理导致了Env抗原性的变化，类似于与戊二醛固定有关的变化。显然，HIV-1Env前体的蛋白降解处理降低了Env三聚体复合体的构象灵活性，从而不同地影响中和抗体和非中和抗体表位的完整性/可及性。
The mature envelope glycoprotein (Env) spike on the surface of human immunodeficiency virus type 1 (HIV-1) virions is derived by proteolytic cleavage of a trimeric gp160 glycoprotein precursor. Remarkably, proteolytic processing of the HIV-1 Env precursor results in changes in Env antigenicity that resemble those associated with glutaraldehyde fixation. Apparently, proteolytic processing of the HIV-1 Env precursor decreases conformational flexibility of the Env trimeric complex, differentially affecting the integrity/accessibility of epitopes for neutralizing and nonneutralizing antibodies.