Important note: Information in this article was accurate in 1992. The state of the art may have changed since the publication date.
CHARACTERIZATION OF ENVELOPE GLYCOPROTEIN PROCESSING AND FUSION DOMAINS OF MURINE AND HUMAN RETROVIRUSES
Diss Abstr Int [B]; 51(11):5158 1991. Unique Identifier : AIDSLINE ICDB/92677006 Freed EO; Univ. of Wisconsin - Madison
Abstract:
Envelope glycoproteins play a central role in several stages of the retroviral life cycle. They bear the domains responsible for binding cell surface receptors, and they initiate the fusion between the viral envelope and the host cell membrane. Retroviral envelope glycoproteins also induce cell fusion, and they may therefore contribute to the pathogenesis following retroviral infection. An Arg to Lys mutation was transferred from the endogenous ecotropic virus of the BALB/c strain of mouse to the endogenous ecotropic virus of the AKR strain of mouse. The presence of this Lys at the site of processing of the murine leukemia virus envelope glycoprotein precursor greatly reduced precursor processing and rendered the mutant virus unable to induce the XC cell fusion. Mutations were also introduced into the processing sequence of the envelope glycoprotein precursor of the human immunodeficiency virus type 1 (HIV-1). The results indicated that an Arg to Thr mutation at the cleavage site blocked precursor processing, that a basic pair of amino acids at the cleavage site was not absolutely required for envelope precursor processing, and that a block in precursor processing rendered the envelope glycoprotein unable to induce cell fusion. For this work, three vectors were developed for the efficient expression of HIV-1 envelope glycoproteins in the absence of viral replication. To examine further the cell fusion function of the HIV-1 envelope glycoproteins, mutations were introduced into the hydrophobic amino terminus of the transmembrane glycoprotein gp41 and into the major neutralizing domain (the V3 loop) of the surface glycoprotein gp120. Both of these domains were shown to be involved in the cell fusion function of the HIV-1 envelope glycoproteins. (Full text available from University Microfilms International, Ann Arbor, MI, as Order No. AAD91-08265).
Keywords: *Cell Fusion Glycoproteins/*METABOLISM HIV Envelope Protein gp120/METABOLISM HIV Envelope Protein gp41/METABOLISM Mice, Inbred BALB C Mutation Protein Precursors/METABOLISM Retroviridae Proteins/*METABOLISM Viral Envelope Proteins/*METABOLISM THESIS
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Important note: Information in this article was accurate in 1992. The state of the art may have changed since the publication date.
