气候变化领域集成服务门户(CCPortal): Recapitulation of HIV-1 Env-antibody coevolution in macaques leading to neutralization breadth

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DOI	10.1126/science.abd2638
	Recapitulation of HIV-1 Env-antibody coevolution in macaques leading to neutralization breadth
	Roark R.S.; Li H.; Williams W.B.; Chug H.; Mason R.D.; Gorman J.; Wang S.; Lee F.-H.; Rando J.; Bonsignori M.; Hwang K.-K.; Saunders K.O.; Wiehe K.; Moody M.A.; Hraber P.T.; Wagh K.; Giorgi E.E.; Russell R.M.; Bibollet-Ruche F.; Liu W.; Connel J.; Smith A.G.; DeVoto J.; Murphy A.I.; Smith J.; Ding W.; Zhao C.; Chohan N.; Okumura M.; Rosario C.; Ding Y.; Lindemuth E.; Bauer A.M.; Bar K.J.; Ambrozak D.; Chao C.W.; Chuang G.-Y.; Geng H.; Lin B.C.; Louder M.K.; Nguyen R.; Zhang B.; Lewis M.G.; Raymond D.D.; Doria-Rose N.A.; Schramm C.A.; Douek D.C.; Roederer M.; Kepler T.B.; Kelsoe G.; Mascola J.R.; Kwong P.D.; Korber B.T.; Harrison S.C.; Haynes B.F.; Hahn B.H.; Shaw G.M.
发表日期	2021
ISSN	0036-8075
卷号	371 期号:6525
英文摘要	Neutralizing antibodies elicited by HIV-1 coevolve with viral envelope proteins (Env) in distinctive patterns, in some cases acquiring substantial breadth. We report that primary HIV-1 envelope proteins - when expressed by simian-human immunodeficiency viruses in rhesus macaques - elicited patterns of Env-antibody coevolution very similar to those in humans, including conserved immunogenetic, structural, and chemical solutions to epitope recognition and precise Env-amino acid substitutions, insertions, and deletions leading to virus persistence. The structure of one rhesus antibody, capable of neutralizing 49% of a 208-strain panel, revealed a V2 apex mode of recognition like that of human broadly neutralizing antibodies (bNAbs) PGT145 and PCT64-35S. Another rhesus antibody bound the CD4 binding site by CD4 mimicry, mirroring human bNAbs 8ANC131, CH235, and VRC01. Virus-antibody coevolution in macaques can thus recapitulate developmental features of human bNAbs, thereby guiding HIV-1 immunogen design. Copyright © 2021, American Association for the Advancement of Science.
英文关键词	arginine; broadly neutralizing antibody; CD4 antibody; CD4 antigen; DNA; epitope; Human immunodeficiency virus antibody; immunoglobulin G; lysine; monoclonal antibody; monoclonal antibody 8ANC131; monoclonal antibody CH106; monoclonal antibody CH235; monoclonal antibody VRC01; unclassified drug; virus envelope protein; CD4 antigen; epitope; glycoprotein gp 120; antibody; coevolution; human immunodeficiency virus; primate; amino acid substitution; animal cell; animal experiment; animal model; antibody affinity; antibody production; antibody response; antibody titer; antigen antibody complex; antigen binding; antigen recognition; antigenicity; Article; B lymphocyte; binding site; bioinformatics; CD4+ T lymphocyte; cell lineage; coevolution; conformational transition; controlled study; crystal structure; DNA sequence; drug design; genetic conservation; high throughput sequencing; human; Human immunodeficiency virus 1 infection; IC50; immunogenetics; indel mutation; molecular mimicry; nonhuman; peripheral blood mononuclear cell; persistent virus infection; primate disease; priority journal; rhesus monkey; site directed mutagenesis; vaccination; vaccine production; virus entry; virus load; virus mutation; virus neutralization; virus replication; virus strain; X ray diffraction; animal; chemistry; coevolution; cryoelectron microscopy; genetics; Human immunodeficiency virus 1; Human immunodeficiency virus infection; immunology; Simian immunodeficiency virus; Macaca; Macaca mulatta; Animals; Binding Sites; Biological Coevolution; Broadly Neutralizing Antibodies; CD4 Antigens; Cryoelectron Microscopy; Epitopes; HIV Antibodies; HIV Envelope Protein gp120; HIV Infections; HIV-1; Humans; Macaca mulatta; Molecular Mimicry; Simian Immunodeficiency Virus; Virus Replication
语种	英语
来源期刊	Science
文献类型	期刊论文
条目标识符	http://gcip.llas.ac.cn/handle/2XKMVOVA/245238
作者单位	Departments of Medicine and Microbiology, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA 19104, United States; Duke Human Vaccine Institute, Duke University School of Medicine, Durham, NC 27710, United States; Department of Medicine, Duke University School of Medicine, Durham, NC 27710, United States; Laboratory of Molecular Medicine, Boston Children's Hospital, Harvard Medical School, Boston, MA 02115, United States; Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, United States; Departments of Immunology and Surgery, Duke University School of Medicine, Durham, NC 27710, United States; Departments of Pediatrics and Immunology, Duke University School of Medicine, Durham, NC 27710, United States; Theoretical Biology and Biophysics, Los Alamos National Laboratory, Los Alamos, NM 87545, United States; Bioqual, Inc., Rockville, MD 20850, United States; Department of Microbiology, Boston Univer...
推荐引用方式 GB/T 7714	Roark R.S.,Li H.,Williams W.B.,et al. Recapitulation of HIV-1 Env-antibody coevolution in macaques leading to neutralization breadth[J],2021,371(6525).
APA	Roark R.S..,Li H..,Williams W.B..,Chug H..,Mason R.D..,...&Shaw G.M..(2021).Recapitulation of HIV-1 Env-antibody coevolution in macaques leading to neutralization breadth.Science,371(6525).
MLA	Roark R.S.,et al."Recapitulation of HIV-1 Env-antibody coevolution in macaques leading to neutralization breadth".Science 371.6525(2021).