Reply to “The Broadly Neutralizing, Anti-HIV Antibody 4E10: an Open and Shut Case?”

descriptionPublicationkeyboard_double_arrow_right Article 15 Mar 2016 English Publisher:American Society for MicrobiologyJournal:Journal of Virology, volume 90, pages 3,276-3,277 (issn: 0022-538X, eissn: 1098-5514,

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Authors: Edurne Rujas; Naveed Gulzar; Koldo Morante; Kouhei Tsumoto; Jamie K. Scott; José L. Nieva; Jose M. M. Caaveiro;

doi: 10.1128/jvi.02970-15

pmid: 26921373

pmc: PMC4810630

Reply to “The Broadly Neutralizing, Anti-HIV Antibody 4E10: an Open and Shut Case?”

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Abstract

We thank Drs. Strong and Finton for their interest in our work involving the broadly neutralizing anti-HIV-1 antibody 4E10 ([1][1]). In that study, we determined the crystal structure of the unbound form of the Fab region of 4E10, as well as that of nonneutralizing mutants with the peptide epitope

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Keywords

Models, Molecular, Epitopes, Antibodies, Monoclonal, Humans, HIV Antibodies, Antibodies, Neutralizing, HIV Envelope Protein gp41

2 Research products, page 1 of 1

Structural and Thermodynamic Basis of Epitope Binding by Neutralizing and Nonneutralizing Forms of the Anti-HIV-1 Antibody 4E10
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Crystal structure of broadly neutralizing anti-hiv-1 antibody 4e10, mutant npro, with peptide bound
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