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Varying effects of temperature, Ca 2+ and cytochalasin on fusion activity mediated by human immunodeficiency virus type 1 and type 2 glycoproteins
Author(s) -
Jernigan Kristine M,
Blumenthal Robert,
Puri Anu
Publication year - 2000
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/s0014-5793(00)01600-8
Subject(s) - glycoprotein , cell fusion , hela , lipid bilayer fusion , viral envelope , cytochalasin , fusion , herpesvirus glycoprotein b , chemistry , virology , cytochalasin b , cytochalasin d , microbiology and biotechnology , virus , biology , biophysics , in vitro , biochemistry , viral entry , cell , viral replication , cytoskeleton , linguistics , philosophy
We examined fusion mediated by the human immunodeficiency virus type 1 (HIV‐1) and type 2 (HIV‐2) envelope glycoproteins under various experimental conditions. Incubation of HeLa cells expressing HIV‐2 ROD and HIV‐2 SBL/ISY envelope glycoproteins with HeLa‐CD4 target cells resulted in fusion at temperatures ≥25°C whereas fusion with cells expressing HIV‐1 Lai occurred only at ≥31°C. HIV‐2 envelope glycoprotein‐mediated fusion proceeded in the absence of Ca 2+ in the culture medium, whereas HIV‐1 fusion required Ca 2+ ions for fusion. In contrast to HIV‐2 envelope glycoprotein fusion, incubations in the presence of the 0.5 μM cytochalasin B completely inhibited HIV‐1 envelope glycoprotein‐mediated fusion. Our results suggest that in contrast to HIV‐2, HIV‐1 fusion is dependent on dynamic processes in the target membrane.