This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Freed, E O Articles by Myers, D J Search for Related Content PubMed PubMed Citation Articles by Freed, E O Articles by Myers, D J

Identification and characterization of fusion and processing domains of the human immunodeficiency virus type 2 envelope glycoprotein.

McArdle Laboratory for Cancer Research, University of Wisconsin, Madison 53706.

ABSTRACT

The envelope glycoprotein of the human immunodeficiency virus type 2 (HIV-2) is synthesized as a polyprotein precursor which is proteolytically processed to produce the mature surface and transmembrane envelope glycoproteins. The processed envelope glycoprotein species are responsible for the fusion between the viral envelope and the host cell membrane during the infection process. The envelope glycoprotein also induces syncytium formation between envelope-expressing cells and receptor-bearing cells. To characterize domains of the HIV-2 envelope glycoprotein involved in membrane fusion and in proteolytic processing, we introduced single amino acid mutations into the region of the HIV-2 surface glycoprotein corresponding to the principal neutralizing determinant (the V3 loop) of HIV-1, the putative HIV-2 envelope precursor-processing sequence, and the hydrophobic amino terminus of the HIV-2 transmembrane envelope glycoprotein. The effects of these mutations on syncytium formation, virus infectivity, envelope expression, envelope processing, and CD4 binding were analyzed. Our results suggest that the V3-like region of the HIV-2 surface glycoprotein and the hydrophobic amino terminus of the transmembrane glycoprotein are HIV-2 fusion domains and characterize the effects of mutations in the HIV-2 envelope glycoprotein precursor-processing sequence.

This article has been cited by other articles:

• Lerner, D. L., Elder, J. H. (2000). Expanded Host Cell Tropism and Cytopathic Properties of Feline Immunodeficiency Virus Strain PPR Subsequent to Passage through Interleukin-2-Independent T Cells. J. Virol. 74: 1854-1863 [Abstract] [Full Text]  
• Ito, H., Watanabe, S., Sanchez, A., Whitt, M. A., Kawaoka, Y. (1999). Mutational Analysis of the Putative Fusion Domain of Ebola Virus Glycoprotein. J. Virol. 73: 8907-8912 [Abstract] [Full Text]  
• Mörner, A., Björndal, A., Albert, J., KewalRamani, V. N., Littman, D. R., Inoue, R., Thorstensson, R., Fenyö, E. M., Björling, E. (1999). Primary Human Immunodeficiency Virus Type 2 (HIV-2) Isolates, Like HIV-1 Isolates, Frequently Use CCR5 but Show Promiscuity in Coreceptor Usage. J. Virol. 73: 2343-2349 [Abstract] [Full Text]  
• Freed, E. O., Martin, M. A. (1995). The Role of Human Immunodeficiency Virus Type 1 Envelope Glycoproteins in Virus Infection. J. Biol. Chem. 270: 23883-23886 [Full Text]