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PMID: 7815477 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Proteinase-resistant factors in human erythrocyte membranes mediate CD4-dependent fusion with cells expressing human immunodeficiency virus type 1 envelope glycoproteins.

Journal of virology ·Vol. 69 ·No. 2 ·1995-02-00 ·Pages 1013-8

Dragic T, Picard L, Alizon M

Abstract

Murine CD4+ cells are resistant to human immunodeficiency virus type 1 (HIV-1) entry and to fusion with cells expressing HIV-1 envelope glycoproteins (Env). The role of human-specific factors in Env/CD4-mediated fusion is shown by the ability of transient cell hybrids formed between CD4+ murine cells and human HeLa cells to fuse with Env+ cells. Fusion events were observed when other human cells, including erythrocytes, were substituted for HeLa cells in the hybrids. Experiments with erythrocyte ghosts showed that the factors allowing Env/CD4-mediated fusion are located in the plasma membrane. These factors were fully active after extensive digestion of erythrocytes with proteinase K or pronase. Nonprotein components of human plasma membranes, possibly glycolipids, could therefore be required for Env/CD4-mediated fusion and virus entry.

MeSH Terms
3T3 Cells Animals CD4 Antigens/physiology Cell Line Endopeptidase K Erythrocyte Membrane/physiology Gene Products, env/physiology HIV-1/physiology Humans Leukemia, Erythroblastic, Acute/pathology Membrane Fusion Mice Pronase/pharmacology Serine Endopeptidases/pharmacology
Chemicals
CD4 Antigens Gene Products, env Serine Endopeptidases Endopeptidase K Pronase
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Dragic T
Institut National de la Santé et de la Recherche Médicale U332, Institut Cochin de Génétique Moléculaire, Paris, France.
Picard L
Alizon M
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Article Info
Journal
Journal of virology
Abbr.
J Virol
ISSN
0022-538X
DOI
10.1128/JVI.69.2.1013-1018.1995
Published
1995-02-00
Pages
1013-8
Language
English
Region
United States
NLM ID
0113724
PMCID
PMC188670
Subset
IM
External Links
PubMed source DOI: 10.1128/JVI.69.2.1013-1018.1995 PMC Full Text View journal details
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