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Full-Text Articles in Virology
Contribution Of The Gp120 V3 Loop To Envelope Glycoprotein Trimer Stability In Primate Immunodeficiency Viruses, Dane Bowder, Haley Hollingsead, Kate Durst, Duoyi Hu, Wenzhong Wei, Joshua Wiggins, Halima Medjahed, Andrés Finzi, Joseph Sodroski, Shi-Hua Xiang
Contribution Of The Gp120 V3 Loop To Envelope Glycoprotein Trimer Stability In Primate Immunodeficiency Viruses, Dane Bowder, Haley Hollingsead, Kate Durst, Duoyi Hu, Wenzhong Wei, Joshua Wiggins, Halima Medjahed, Andrés Finzi, Joseph Sodroski, Shi-Hua Xiang
Nebraska Center for Virology: Faculty Publications
The V3 loop of the human immunodeficiency virus type 1 (HIV-1) gp120 exterior envelope glycoprotein (Env) becomes exposed after CD4 binding and contacts the coreceptor to mediate viral entry. Prior to CD4 engagement, a hydrophobic patch located at the tip of the V3 loop stabilizes the non-covalent association of gp120 with the Env trimer of HIV-1 subtype B strains. Here, we show that this conserved hydrophobic patch (amino acid residues 307, 309 and 317) contributes to gp120-trimer association in HIV-1 subtype C, HIV-2 and SIV. Changes that reduced the hydrophobicity of these V3 residues resulted in increased gp120 shedding and …
Analysis Of Hiv-2 Vpx By Modeling And Insertional Mutagenesis, Lisa A. Mahnke, Michael Belshan, Lee Ratner
Analysis Of Hiv-2 Vpx By Modeling And Insertional Mutagenesis, Lisa A. Mahnke, Michael Belshan, Lee Ratner
Nebraska Center for Virology: Faculty Publications
Vpx facilitates HIV-2 nuclear localization by a poorly understood mechanism. We have compared Vpx to an NMR structure HIV- 1 Vpr in a central helical domain and probed regions of Vpx by insertional mutagenesis. A predicted loop between helices two and three appears to be unique, overlapping with a known novel nuclear localization signal. Overall, Vpx was found to be surprisingly flexible, tolerating a series of large insertions. We found that insertion within the polyproline-containing C-terminus destabilizes nuclear localization, whereas mutating a second helix in the central domain disrupts viral packaging. Other insertional mutants in the predicted loop and in …
Conserved Amino Acids Of The Human Immunodeficiency Virus Type 2 Vpx Nuclear Localization Signal Are Critical For Nuclear Targeting Of The Viral Preintegration Complex In Non-Dividing Cells, Michael Belshan, Lisa A. Mahnke, Lee Ratner
Conserved Amino Acids Of The Human Immunodeficiency Virus Type 2 Vpx Nuclear Localization Signal Are Critical For Nuclear Targeting Of The Viral Preintegration Complex In Non-Dividing Cells, Michael Belshan, Lisa A. Mahnke, Lee Ratner
Nebraska Center for Virology: Faculty Publications
The HIV-2 viral accessory protein Vpx is related to, but distinct from the Vpr protein of HIV-1. Vpx is packaged into virions and as a component of the viral preintegration complex (PIC) is required for efficient virus replication in non-dividing cells. We have previously reported that the minimal transferable region of Vpx that contained karyophilic properties was aa 65 to 72. Analysis of Vpx sequences from various HIV-2/SIV strains reveals that this region contains highly conserved amino acids, including two basic residues (K68, R70) and three tyrosines (Y66, Y69, Y71). Here, we demonstrate that mutation of the basic or tyrosine …