Willey R L, Bonifacino J S, Potts B J, Martin M A, Klausner R D
Laboratory of Molecular Microbiology, National Institute of Allergy and Infectious Diseases, Bethesda, MD 20892.
Proc Natl Acad Sci U S A. 1988 Dec;85(24):9580-4. doi: 10.1073/pnas.85.24.9580.
The synthesis and processing of the human immunodeficiency virus 1 (HIV-1) envelope precursor glycoprotein gp 160 was studied in an infected CD4+ lymphocytic cell line. Surprisingly, only a small percentage (5-15%) of gp160 is cleaved to produce the mature gp120 component. Intracellular sorting results in the transfer of most uncleaved gp160 to lysosomes, where it is degraded, while gp120 is transported to the cell surface and subsequently secreted. Cleavage of gp160 to generate gp120 occurs intracellularly and can be inhibited by NH4Cl. Taken together, these results indicate that intracellular cleavage of gp160 determines the intracellular transport and survival of the envelope glycoproteins necessary to produce infectious virus.
在一个受感染的CD4 +淋巴细胞系中研究了人类免疫缺陷病毒1型（HIV-1）包膜前体糖蛋白gp160的合成与加工。令人惊讶的是，只有一小部分（5-15%）的gp160被切割产生成熟的gp120组分。细胞内分选导致大多数未切割的gp160转移至溶酶体并在那里被降解，而gp120则被转运至细胞表面并随后分泌。gp160切割产生gp120的过程发生在细胞内，并且可被NH4Cl抑制。综上所述，这些结果表明gp160的细胞内切割决定了产生感染性病毒所必需的包膜糖蛋白的细胞内转运和存活。
