Document 0189
 DOCN  M9440189
 TI    gp120-independent fusion mediated by the human immunodeficiency virus
       type 1 gp41 envelope glycoprotein: a reassessment.
 DT    9404
 AU    Marcon L; Sodroski J; Dana-Farber Cancer Institute, Department of
       Pathology, Harvard; Medical School, Boston, Massachusetts 02115.
 SO    J Virol. 1994 Mar;68(3):1977-82. Unique Identifier : AIDSLINE
       MED/94149895
 AB    In a natural context, membrane fusion mediated by the human
       immunodeficiency virus type 1 (HIV-1) envelope glycoproteins involves
       both the exterior envelope glycoprotein (gp120) and the transmembrane
       glycoprotein (gp41). Perez et al. (J. Virol. 66:4134-4143, 1992)
       reported that a mutant HIV-1 envelope glycoprotein containing only the
       signal peptide and carboxyl terminus of the gp120 exterior glycoprotein
       fused to the complete gp41 glycoprotein was properly cleaved and that
       the resultant gp41 glycoprotein was able to induce the fusion of even
       CD4-negative cells. In the studies reported herein, mutant proteins
       identical or similar to those studied by Perez et al. lacked detectable
       cell fusion activity. The proteolytic processing of these proteins was
       very inefficient, and one processed product identified by Perez et al.
       as the authentic gp41 glycoprotein was shown to contain
       carboxyl-terminal gp120 sequences. Furthermore, no fusion activity was
       observed for gp41 glycoproteins exposed after shedding of the gp120
       glycoprotein by soluble CD4. Thus, evidence supporting a
       gp120-independent cell fusion activity for the HIV-1 gp41 glycoprotein
       is currently lacking.
 DE    Amino Acid Sequence  Antigens, CD4/PHARMACOLOGY  Cell Fusion/DRUG
       EFFECTS  Hela Cells  Human  HIV Envelope Protein
       gp120/PHARMACOLOGY/*PHYSIOLOGY  HIV Envelope Protein
       gp41/PHARMACOLOGY/*PHYSIOLOGY  HIV-1/*PHYSIOLOGY  *Membrane Fusion
       Molecular Sequence Data  Sequence Deletion  Support, Non-U.S. Gov't
       Support, U.S. Gov't, P.H.S.  Viral Fusion
       Proteins/PHARMACOLOGY/*PHYSIOLOGY  JOURNAL ARTICLE

       SOURCE: National Library of Medicine.  NOTICE: This material may be
       protected by Copyright Law (Title 17, U.S.Code).