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1. Anti-V2 antibodies virus vulnerability revealed by envelope V1 deletion in HIV vaccine candidates.

Author

Silva de Castro I, Gorini G, Mason R, Gorman J, Bissa M, Rahman MA, Arakelyan A, Kalisz I, Whitney S, Becerra-Flores M, Ni E, Peachman K, Trinh HV, Read M, Liu MH, Van Ryk D, Paquin-Proulx D, Shubin Z, Tuyishime M, Peele J, Ahmadi MS, Verardi R, Hill J, Beddall M, Nguyen R, Stamos JD, Fujikawa D, Min S, Schifanella L, Vaccari M, Galli V, Doster MN, Liyanage NPM, Sarkis S, Caccuri F, LaBranche C, Montefiori DC, Tomaras GD, Shen X, Rosati M, Felber BK, Pavlakis GN, Venzon DJ, Magnanelli W, Breed M, Kramer J, Keele BF, Eller MA, Cicala C, Arthos J, Ferrari G, Margolis L, Robert-Guroff M, Kwong PD, Roederer M, Rao M, Cardozo TJ, and Franchini G

Abstract

The efficacy of ALVAC-based HIV and SIV vaccines in humans and macaques correlates with antibodies to envelope variable region 2 (V2). We show here that vaccine-induced antibodies to SIV variable region 1 (V1) inhibit anti-V2 antibody-mediated cytotoxicity and reverse their ability to block V2 peptide interaction with the α 4 β 7 integrin. SIV vaccines engineered to delete V1 and favor an α helix, rather than a β sheet V2 conformation, induced V2-specific ADCC correlating with decreased risk of SIV acquisition. Removal of V1 from the HIV-1 clade A/E A244 envelope resulted in decreased binding to antibodies recognizing V2 in the β sheet conformation. Thus, deletion of V1 in HIV envelope immunogens may improve antibody responses to V2 virus vulnerability sites and increase the efficacy of HIV vaccine candidates., Competing Interests: The US Government has filed a patent on the V1-deleted immunogens with G.F., T.C., I.S.d.C., M.B.-F., M. Bissa., and R.M.A as inventors., (© 2021.)

Published
2021
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2. Compensatory changes in the cytoplasmic tail of gp41 confer resistance to tetherin/BST-2 in a pathogenic nef-deleted SIV.

Author

Serra-Moreno R, Jia B, Breed M, Alvarez X, and Evans DT

Subjects
Animals, Cells, Cultured, Host-Pathogen Interactions, Leukocytes, Mononuclear immunology, Leukocytes, Mononuclear virology, Macaca mulatta immunology, Molecular Sequence Data, Mutant Proteins genetics, Mutant Proteins metabolism, Sequence Analysis, DNA, Simian Immunodeficiency Virus immunology, Antigens, CD immunology, Macaca mulatta virology, Membrane Glycoproteins genetics, Membrane Glycoproteins metabolism, Mutation, Missense, Retroviridae Proteins genetics, Retroviridae Proteins metabolism, Simian Immunodeficiency Virus pathogenicity, Viral Regulatory and Accessory Proteins deficiency
Abstract

Tetherin (BST-2 or CD317) is an interferon-inducible transmembrane protein that inhibits virus release from infected cells. Whereas HIV-1 Vpu and HIV-2 Env counteract human tetherin, most SIVs use Nef to antagonize the tetherin proteins of their nonhuman primate hosts. Here, we show that compensatory changes in the cytoplasmic domain of SIV gp41, acquired by a nef-deleted virus that regained a pathogenic phenotype in infected rhesus macaques, restore resistance to tetherin. These changes facilitate virus release in the presence of rhesus tetherin, but not human tetherin, and enhance virus replication in interferon-treated primary lymphocytes. The substitutions in gp41 result in a selective physical association with rhesus tetherin, and the internalization and sequestration of rhesus tetherin by a mechanism that depends on a conserved endocytosis motif in gp41. These results are consistent with HIV-2 Env antagonism of human tetherin and suggest that the ability to oppose tetherin is important for lentiviral pathogenesis., (Copyright © 2011 Elsevier Inc. All rights reserved.)

Published
2011
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