The Broadly Neutralizing, Anti-HIV Antibody 4E10: an Open and Shut Case?
作者信息
Strong Roland K, Finton Kathryn A K
机构信息
Division of Basic Sciences, Fred Hutchinson Cancer Research Center, Seattle, Washington, USA
Division of Basic Sciences, Fred Hutchinson Cancer Research Center, Seattle, Washington, USA.
出版信息
J Virol. 2016 Feb 26;90(6):3274-5. doi: 10.1128/JVI.02935-15. Print 2016 Mar.
Abstract
摘要
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引用本文的文献
1
Reply to "The Broadly Neutralizing, Anti-HIV Antibody 4E10: an Open and Shut Case?".
J Virol. 2016 Feb 26;90(6):3276-7. doi: 10.1128/JVI.02970-15. Print 2016 Mar.
本文引用的文献
1
Structural and Thermodynamic Basis of Epitope Binding by Neutralizing and Nonneutralizing Forms of the Anti-HIV-1 Antibody 4E10.
J Virol. 2015 Dec;89(23):11975-89. doi: 10.1128/JVI.01793-15. Epub 2015 Sep 16.
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Stapled HIV-1 peptides recapitulate antigenic structures and engage broadly neutralizing antibodies.
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Ontogeny of recognition specificity and functionality for the broadly neutralizing anti-HIV antibody 4E10.
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Autoreactivity and exceptional CDR plasticity (but not unusual polyspecificity) hinder elicitation of the anti-HIV antibody 4E10.
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Role of HIV membrane in neutralization by two broadly neutralizing antibodies.
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Interactions between lipids and human anti-HIV antibody 4E10 can be reduced without ablating neutralizing activity.
J Virol. 2010 Jan;84(2):1076-88. doi: 10.1128/JVI.02113-09. Epub 2009 Nov 11.
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Structural basis of enhanced binding of extended and helically constrained peptide epitopes of the broadly neutralizing HIV-1 antibody 4E10.
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Domain interactions in the Fab fragment: a comparative evaluation of the single-chain Fv and Fab format engineered with variable domains of different stability.
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