The p2 domain of human immunodeficiency virus type 1 Gag regulates sequential proteolytic processing and is required to produce fully infectious virions.
作者： S C Pettit , M D Moody , R S Wehbie , A H Kaplan , P V Nantermet
DOI: 10.1128/JVI.68.12.8017-8027.1994
关键词:
摘要: The proteolytic processing sites of the human immunodeficiency virus type 1 (HIV-1) Gag precursor are cleaved in a sequential manner by viral protease. We investigated factors that regulate processing. When full-length protein was digested with recombinant HIV-1 protease vitro, four five major were at rates differ as much 400-fold. Three these independently others. CA/p2 site, however, approximately 20-fold faster when adjacent downstream p2/NC site blocked from cleavage or p2 domain deleted. These results suggest presence C-terminal tail on intermediates slows upstream site. also found lower pH selectively accelerated and peptide primarily sequence-based mechanism rather than change conformation. Deletion released virions less infectious despite processed final products Gag. findings regulates rate during vitro infected cells may function proper assembly virions.
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