Literature DB >> 9188654

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

R J Center1, B E Kemp, P 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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Year:  1997        PMID： 9188654      PMCID： PMC191822          DOI： 10.1128/JVI.71.7.5706-5711.1997

Source DB:  PubMed          Journal:  J Virol        ISSN： 0022-538X            Impact factor:   5.103


  44 in total

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Authors:  K Salzwedel; E A Berger
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7.  Functional domains in the retroviral transmembrane protein.

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8.  Promoting trimerization of soluble human immunodeficiency virus type 1 (HIV-1) Env through the use of HIV-1/simian immunodeficiency virus chimeras.

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9.  Functional complementation of a model target to study Vpu sensitivity.

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