Glycoprotein incorporation and HIV-1 infectivity despite exchange of the gp160 membrane-spanning domain

Virology
T WilkV Bosch

Abstract

We have examined the role of the membrane-anchoring domain of the HIV-1 glycoproteins in viral glycoprotein function, glycoprotein incorporation, and viral infectivity. For this purpose, we initially exchanged the entire membrane-spanning region with that from a cellular glycoprotein (CD22). Subsequently, the strictly conserved arginine in the central position of the transmembranal alpha-helix was replaced by a neutral residue (R696 --> I696). We have further examined the requirements within the cytoplasmic C-terminus for glycoprotein incorporation and replaced this region of gp160 with the long cytoplasmic C-terminus (118 amino acids) from CD22. Our results show that the specific amino acid sequence of the membrane-spanning region of gp160 is not necessary for viral infectivity, thus making it unlikely that this region is specifically involved in membrane fusion, in glycoprotein incorporation, or in infectivity of the cell lines tested. In contrast, recombinant gp160 with the CD22 C-terminal region, although present at the cell surface and membrane fusion-competent, was excluded from incorporation into particles. This could indicate that steric exclusion, and no pseudotyping, occurs when the heterologous, cytoplasmic C-termina...Continue Reading

Citations

Jul 18, 2012·Proceedings of the National Academy of Sciences of the United States of America·Tina Y LiuJunjie Hu
Mar 10, 2000·AIDS Research and Human Retroviruses·Q YaoC Chen
Sep 3, 1999·Molecular Biology of the Cell·G M Taylor, D A Sanders
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Dec 2, 2010·Retrovirology·Shujun LiuZene Matsuda
Aug 5, 1997·Proceedings of the National Academy of Sciences of the United States of America·B S SchnierleK Cichutek
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