PMID: 9188654Jul 1, 1997Paper

Human immunodeficiency virus type 1 and 2 envelope glycoproteins oligomerize through conserved sequences

Journal of Virology
R J CenterP Poumbourios

Abstract

Hetero-oligomerization between human immunodeficiency virus type 2 (HIV-2) envelope glycoprotein (Env) truncation mutants and epitope-tagged gp160 is dependent on the presence of gp41 transmembrane protein (TM) amino acids 552 to 589, a putative amphipathic alpha-helical sequence. HIV-2 Env truncation mutants containing this sequence were also able to form cross-type hetero-oligomers with HIV-1 Env. HIV-2/HIV-1 hetero-oligomerization was, however, more sensitive to disruption by mutagenesis or increased temperature. The conservation of the Env oligomerization function of the HIV-1 and HIV-2 alpha-helical sequences suggests that retroviral TM alpha-helical motifs may have a universal role in oligomerization.

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Citations

Apr 2, 2011·AIDS Research and Human Retroviruses·Sushama JadhavRamesh Paranjape
Jul 31, 1998·Protein Science : a Publication of the Protein Society·R J CenterP Poumbourios
Dec 26, 2001·Proceedings of the National Academy of Sciences of the United States of America·R J CenterJ Lebowitz
Dec 3, 2004·The Journal of Biological Chemistry·Oliver LenzWinfried Weissenhorn
Jul 11, 2013·PloS One·Sanath Kumar JanakaMarc C Johnson
Oct 26, 2000·Proceedings of the National Academy of Sciences of the United States of America·K Salzwedel, E A Berger
Jun 17, 1998·Journal of Virology·Y ZhaoP M Cannon

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