Publications & Reports

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

R J Center, B E Kemp, P Poumbourios
St. Vincent's Institute of Medical Research, Fitzroy, Victoria, Australia.

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 ™ 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.

Publication

  • Journal: Journal of virology
  • Published: 01/07/1997
  • Volume: 71
  • Issue: 7
  • Pagination: 5706-5711

Authors

Health Issue