Molecular simulations and modeling of HIV-1 gp41 membrane spanning domain (MSD) in a model viral bilayer

2021 ◽  
Author(s):  
Michelle Katherine Baker
Keyword(s):  
Molecular Simulations ◽  
Membrane Spanning ◽  
Simulations And Modeling ◽  
Hiv 1

scholarly journals In Silico Vaccine Design Based on Molecular Simulations of Rhinovirus Chimeras Presenting HIV-1 gp41 Epitopes

2009 ◽  
Vol 385 (2) ◽  
pp. 675-691 ◽  
Author(s):  
Mauro Lapelosa ◽  
Emilio Gallicchio ◽  
Gail Ferstandig Arnold ◽  
Eddy Arnold ◽  
Ronald M. Levy
Keyword(s):  
In Silico ◽  
Molecular Simulations ◽  
Vaccine Design ◽  
Hiv 1

scholarly journals Molecular simulations of conformation change and aggregation of HIV-1 Vpr13-33 on graphene oxide

2016 ◽  
Vol 6 (1) ◽  
Author(s):  
Songwei Zeng ◽  
Guoquan Zhou ◽  
Jianzhong Guo ◽  
Feng Zhou ◽  
Junlang Chen
Keyword(s):  
Graphene Oxide ◽  
Molecular Simulations ◽  
Conformation Change ◽  
Hiv 1

scholarly journals All-Atom Models of the Membrane-Spanning Domain of HIV-1 gp41 from Metadynamics

2010 ◽  
Vol 99 (10) ◽  
pp. 3438-3444 ◽  
Author(s):  
Vamshi K. Gangupomu ◽  
Cameron F. Abrams
Keyword(s):  
Membrane Spanning ◽  
Hiv 1

scholarly journals Role of the Membrane-Spanning Domain of Human Immunodeficiency Virus Type 1 Envelope Glycoprotein in Cell-Cell Fusion and Virus Infection

2008 ◽  
Vol 82 (11) ◽  
pp. 5417-5428 ◽  
Author(s):  
Liang Shang ◽  
Ling Yue ◽  
Eric Hunter
Keyword(s):  
Amino Acid ◽  
Cell Fusion ◽  
Viral Entry ◽  
Envelope Glycoprotein ◽  
Amino Acid Residues ◽  
Immunodeficiency Virus ◽  
Membrane Spanning ◽  
Hiv 1

ABSTRACT The membrane-spanning domain (MSD) of the human immunodeficiency virus type 1 (HIV-1) gp41 glycoprotein is critical for its biological activity. Previous C-terminal truncation studies have predicted an almost invariant core structure of 12 amino acid residues flanked by basic amino acids in the HIV-1 MSD that function to anchor the glycoprotein in the lipid bilayer. To further understand the role of specific amino acids within the MSD core, we initially replaced the core region with 12 leucine residues and then constructed recovery-of-function mutants in which specific amino acid residues (including a GGXXG motif) were reintroduced. We show here that conservation of the MSD core sequence is not required for normal expression, processing, intracellular transport, and incorporation into virions of the envelope glycoprotein (Env). However, the amino acid composition of the MSD core does influence the ability of Env to mediate cell-cell fusion and plays a critical role in the infectivity of HIV-1. Replacement of conserved amino acid residues with leucine blocked virus-to-cell fusion and subsequent viral entry into target cells. This restriction could not be released by C-terminal truncation of the gp41 glycoprotein. These studies imply that the highly conserved core residues of the HIV Env MSD, in addition to serving as a membrane anchor, play an important role in mediating membrane fusion during viral entry.

scholarly journals Structural Plasticity in the Topology of Membrane-Spanning Domain of HIV-1 gp41

2014 ◽  
Vol 106 (2) ◽  
pp. 507a
Author(s):  
Alexander Kyrychenko ◽  
Jing He ◽  
William C. Wimley ◽  
Alexey S. Ladokhin
Keyword(s):  
Structural Plasticity ◽  
Membrane Spanning ◽  
Hiv 1

scholarly journals Determinants for Sensitivity of Human Immunodeficiency Virus Coreceptor CXCR4 to the Bicyclam AMD3100

1998 ◽  
Vol 72 (8) ◽  
pp. 6381-6388 ◽  
Author(s):  
Béatrice Labrosse ◽  
Anne Brelot ◽  
Nikolaus Heveker ◽  
Nathalie Sol ◽  
Dominique Schols ◽  
...  
Keyword(s):  
Human Immunodeficiency Virus ◽  
Electrostatic Interactions ◽  
Hydrophobic Interactions ◽  
Direct Interaction ◽  
Single Amino Acid ◽  
Amino Terminal ◽  
Immunodeficiency Virus ◽  
Hiv Entry ◽  
Membrane Spanning ◽  
Hiv 1

ABSTRACT The bicyclam AMD3100 is a potent and selective inhibitor of the replication of human immunodeficiency virus type 1 and type 2 (HIV-1 and HIV-2). It was recently demonstrated that the compound inhibited HIV entry through CXCR4 but not through CCR5. Selectivity of AMD3100 for CXCR4 was further indicated by its lack of effect on HIV-1 and HIV-2 infection mediated by the CCR5, CCR3, Bonzo, BOB, and US28, coreceptors. AMD3100 completely blocked HIV-1 infection mediated by a mutant CXCR4 bearing a deletion of most of the amino-terminal extracellular domain. In contrast, relative resistance to AMD3100 was conferred by different single amino acid substitutions in the second extracellular loop (ECL2) or in the adjacent membrane-spanning domain, TM4. Only substitutions of a neutral residue for aspartic acid and of a nonaromatic residue for phenylalanine (Phe) were associated with drug resistance. This suggests a direct interaction of AMD3100 with these amino acids rather than indirect effects of their mutation on the CXCR4 structure. The interaction of aspartic acids of ECL2 and TM4 with AMD3100 is consistent with the positive charge of bicyclams, which might block HIV-1 entry by preventing electrostatic interactions between CXCR4 and the HIV-1 envelope protein gp120. Other features of AMD3100 must account for its high antiviral activity, in particular the presence of an aromatic linker between the cyclam units. This aromatic group might engage in hydrophobic interactions with the Phe-X-Phe motifs of ECL2 or TM4. These results confirm the importance of ECL2 for the HIV coreceptor activity of CXCR4.

scholarly journals Pseudotyping Incompatibility between HIV-1 and Gibbon Ape Leukemia Virus Env Is Modulated by Vpu

2009 ◽  
Vol 84 (6) ◽  
pp. 2666-2674 ◽  
Author(s):  
Tiffany M. Lucas ◽  
Terri D. Lyddon ◽  
Paula M. Cannon ◽  
Marc C. Johnson
Keyword(s):  
Leukemia Virus ◽  
Cytoplasmic Tail ◽  
Viral Particles ◽  
Immunodeficiency Virus ◽  
Env Protein ◽  
Membrane Spanning ◽  
Gibbon Ape Leukemia Virus ◽  
Hiv 1 ◽  
Murine Leukemia

ABSTRACT The Env protein from gibbon ape leukemia virus (GaLV) has been shown to be incompatible with human immunodeficiency virus type 1 (HIV-1) in the production of infectious pseudotyped particles. This incompatibility has been mapped to the C-terminal cytoplasmic tail of GaLV Env. Surprisingly, we found that the HIV-1 accessory protein Vpu modulates this incompatibility. The infectivity of HIV-1 pseudotyped with murine leukemia virus (MLV) Env was not affected by Vpu. However, the infectivity of HIV-1 pseudotyped with an MLV Env with the cytoplasmic tail from GaLV Env (MLV/GaLV Env) was restricted 50- to 100-fold by Vpu. A Vpu mutant containing a scrambled membrane-spanning domain, VpuRD, was still able to restrict MLV/GaLV Env, but mutation of the serine residues at positions 52 and 56 completely alleviated the restriction. Loss of infectivity appeared to be caused by reduced MLV/GaLV Env incorporation into viral particles. The mechanism of this downmodulation appears to be distinct from Vpu-mediated CD4 downmodulation because Vpu-expressing cells that failed to produce infectious HIV-1 particles nonetheless continued to display robust surface MLV/GaLV Env expression. In addition, if MLV and HIV-1 were simultaneously introduced into the same cells, only the HIV-1 particle infectivity was restricted by Vpu. Collectively, these data suggest that Vpu modulates the cellular distribution of MLV/GaLV Env, preventing its recruitment to HIV-1 budding sites.

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