Search Results - "Gristick, Harry B."
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SARS-CoV-2 neutralizing antibody structures inform therapeutic strategies
Published in Nature (London) (24-12-2020)“…The coronavirus disease 2019 (COVID-19) pandemic presents an urgent health crisis. Human neutralizing antibodies that target the host ACE2 receptor-binding…”
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Structures of Human Antibodies Bound to SARS-CoV-2 Spike Reveal Common Epitopes and Recurrent Features of Antibodies
Published in Cell (20-08-2020)“…Neutralizing antibody responses to coronaviruses mainly target the receptor-binding domain (RBD) of the trimeric spike. Here, we characterized polyclonal…”
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Cryo-EM structure of a CD4-bound open HIV-1 envelope trimer reveals structural rearrangements of the gp120 V1V2 loop
Published in Proceedings of the National Academy of Sciences - PNAS (15-11-2016)“…The HIV-1 envelope (Env) glycoprotein, a trimer of gp120–gp41 heterodimers, relies on conformational flexibility to function in fusing the viral and host…”
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Restriction of HIV-1 Escape by a Highly Broad and Potent Neutralizing Antibody
Published in Cell (06-02-2020)“…Broadly neutralizing antibodies (bNAbs) represent a promising approach to prevent and treat HIV-1 infection. However, viral escape through mutation of the…”
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Structural characterization of a highly-potent V3-glycan broadly neutralizing antibody bound to natively-glycosylated HIV-1 envelope
Published in Nature communications (28-03-2018)“…Broadly neutralizing antibodies (bNAbs) isolated from HIV-1-infected individuals inform HIV-1 vaccine design efforts. Developing bNAbs with increased efficacy…”
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Neutralizing antibodies induced in immunized macaques recognize the CD4-binding site on an occluded-open HIV-1 envelope trimer
Published in Nature communications (08-02-2022)“…Broadly-neutralizing antibodies (bNAbs) against HIV-1 Env can protect from infection. We characterize Ab1303 and Ab1573, heterologously-neutralizing…”
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HIV-1 CD4-binding site germline antibody–Env structures inform vaccine design
Published in Nature communications (17-10-2022)“…BG24, a VRC01-class broadly neutralizing antibody (bNAb) against HIV-1 Env with relatively few somatic hypermutations (SHMs), represents a promising target for…”
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Crystal structure of ATP-bound Get3–Get4–Get5 complex reveals regulation of Get3 by Get4
Published in Nature structural & molecular biology (01-05-2014)“…Tail-anchor proteins are targeted post-translationally to the endoplasmic reticulum via the conserved GET pathway, in which the Get4–Get5 complex mediates…”
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Asymmetric recognition of HIV-1 Envelope trimer by V1V2 loop-targeting antibodies
Published in eLife (26-05-2017)“…The HIV-1 envelope (Env) glycoprotein binds to host cell receptors to mediate membrane fusion. The prefusion Env trimer is stabilized by V1V2 loops that…”
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A broadly neutralizing macaque monoclonal antibody against the HIV-1 V3-Glycan patch
Published in eLife (21-10-2020)“…A small fraction of HIV-1- infected humans develop broadly neutralizing antibodies (bNAbs) against HIV-1 that protect macaques from simian immunodeficiency HIV…”
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Antibody elicited by HIV-1 immunogen vaccination in macaques displaces Env fusion peptide and destroys a neutralizing epitope
Published in npj vaccines (25-10-2021)“…HIV-1 vaccine design aims to develop an immunogen that elicits broadly neutralizing antibodies against a desired epitope, while eliminating responses to…”
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Natively glycosylated HIV-1 Env structure reveals new mode for antibody recognition of the CD4-binding site
Published in Nature structural & molecular biology (01-10-2016)“…Crystal structures of HIV Env trimer with native glycosylation in complex with neutralizing antibodies reveal a glycan shield of high-mannose and complex-type…”
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Asymmetric opening of HIV-1 Env bound to CD4 and a coreceptor-mimicking antibody
Published in Nature structural & molecular biology (01-12-2019)“…The human immunodeficiency virus (HIV-1) envelope (Env) glycoprotein, a (gp120–gp41) 3 trimer, mediates fusion of viral and host cell membranes after gp120…”
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Immunization expands B cells specific to HIV-1 V3 glycan in mice and macaques
Published in Nature (London) (01-06-2019)“…Broadly neutralizing monoclonal antibodies protect against infection with HIV-1 in animal models, suggesting that a vaccine that elicits these antibodies would…”
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X‐ray and EM structures of a natively glycosylated HIV‐1 envelope trimer
Published in Acta crystallographica. Section D, Biological crystallography. (01-10-2017)“…The structural and biochemical characterization of broadly neutralizing anti‐HIV‐1 antibodies (bNAbs) has been essential in guiding the design of potential…”
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Coexistence of potent HIV-1 broadly neutralizing antibodies and antibody-sensitive viruses in a viremic controller
Published in Science translational medicine (18-01-2017)“…Some HIV-1-infected patients develop broad and potent HIV-1 neutralizing antibodies (bNAbs) that when passively transferred to mice or macaques can treat or…”
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Nanoparticles presenting clusters of CD4 expose a universal vulnerability of HIV-1 by mimicking target cells
Published in Proceedings of the National Academy of Sciences - PNAS (04-08-2020)“…CD4-based decoy approaches against HIV-1 are attractive options for long-term viral control, but initial designs, including soluble CD4 (sCD4) and CD4-Ig, were…”
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Sequential immunization of macaques elicits heterologous neutralizing antibodies targeting the V3-glycan patch of HIV-1 Env
Published in Science translational medicine (24-11-2021)“…Broadly neutralizing antibodies (bNAbs) against HIV-1 develop after prolonged virus and antibody coevolution. Previous studies showed that sequential…”
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Publisher Correction: Asymmetric opening of HIV-1 Env bound to CD4 and a coreceptor-mimicking antibody
Published in Nature structural & molecular biology (01-02-2020)“…An amendment to this paper has been published and can be accessed via a link at the top of the paper…”
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Publisher Correction: Asymmetric opening of HIV-1 Env bound to CD4 and a coreceptor-mimicking antibody
Published in Nature structural & molecular biology (2020)“…An amendment to this paper has been published and can be accessed via a link at the top of the paper…”
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