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Clustered localization of oligomeric Nef protein of human immunodeficiency virus type 1 on the cell surface
Author(s) -
Fujii Yoichi,
Otake Kaori,
Fujita Yoshikazu,
Yamamoto Naoki,
Nagai Yoshiyuki,
Tashiro Masato,
Adachi Akio
Publication year - 1996
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(96)01048-4
Subject(s) - cytotoxic t cell , cytoplasm , human immunodeficiency virus (hiv) , cell , virology , chemistry , monomer , hela , biology , microbiology and biotechnology , virus , biochemistry , polymer , in vitro , organic chemistry
We studied human immunodeficiency virus type 1 (HIV‐1) Nef protein biochemically and histologically. HIV‐1 Nef, derived from baculosystem and from cells infected with HIV‐1, formed homomeric monomers, dimers, trimers, and further polymers. These oligomers were non‐covalently associated. In cells infected with HIV‐1, Nef molecules were clustered at the cell surface as well as cytoplasm. Our previous results have indicated that the Nef on the surface of cells infected with HIV‐1 is cytotoxic against uninfected CD4+ T cells. Thus, it is very likely that the HIV‐1‐mediated cytotoxic reaction is due, at least in part, to the clustered localization of oligomeric Nef on the cell surface.