Role of the carboxy-terminal portion of the HIV-1 transmembrane protein in viral transmission and cytopathogenicity.
The transmembrane glycoprotein (gp41) of human immunodeficiency virus type-1 (HIV-1) has a long cytoplasmic domain of unknown functional significance. To investigate the role of the carboxy-terminal (C-terminal) portion of the HIV-1 envelope protein in viral replication, infectivity, and cytopathogenicity, we examined the properties of a panel of mutants with variable deletions in the 3'-env region. Deletion of the C-terminal 76 amino acids did not abolish production of reverse transcriptase upon transfection of COS-1 cells. Deletion of the C-terminal 6-14 amino acids appeared sufficient to alter the replication pattern, infectivity, and cytopathogenicity of some clones. The data suggest that conformational determinants or specific sequences are responsible for the observed changes, rather than simply the length of the gp41 cytoplasmic tail.
Lee
S J
SJ
Laboratory of Tumor Cell Biology, National Cancer Institute, Bethesda, MD 20892.
Hu
W
W
Fisher
A G
AG
Looney
D J
DJ
Kao
V F
VF
Mitsuya
H
H
Ratner
L
L
Wong-Staal
F
F
D003588:Cytopathogenic Effect, Viral; D006678:HIV / Q000472:pathogenicity* / Q000502:physiology; D015488:HIV Antigens / Q000502:physiology*; D015700:HIV Envelope Protein gp41; D009154:Mutation; D013329:Structure-Activity Relationship; D014759:Viral Envelope Proteins / Q000502:physiology*; D014779:Virus Replication
D015488:HIV Antigens; D015700:HIV Envelope Protein gp41; D014759:Viral Envelope Proteins