Changes in the transmembrane region of the human immunodeficiency virus type 1 gp41 envelope glycoprotein affect membrane fusion.
The charged amino acids near or within the membrane-spanning region of the human immunodeficiency virus type 1 gp41 envelope glycoprotein were altered. Two mutants were defective for syncytium formation and virus replication even though levels of envelope glycoproteins on the cell or virion surface and CD4 binding were comparable to those of the wild-type proteins. Thus, in addition to anchoring the envelope glycoproteins, sequences proximal to the membrane-spanning gp41 region are important for the membrane fusion process.
Helseth
E
E
Dana-Farber Cancer Institute, Department of Pathology, Harvard Medical School, Boston, Massachusetts.
Olshevsky
U
U
Gabuzda
D
D
Ardman
B
B
Haseltine
W
W
Sodroski
J
J
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D002460:Cell Line; D002462:Cell Membrane / Q000502:physiology; D015700:HIV Envelope Protein gp41 / Q000235:genetics* / Q000302:isolation & purification / Q000378:metabolism; D015497:HIV-1 / Q000235:genetics* / Q000502:physiology; D008561:Membrane Fusion; D008969:Molecular Sequence Data; D008970:Molecular Weight; D016297:Mutagenesis, Site-Directed
D015700:HIV Envelope Protein gp41