Anti-peptide antibodies detect steps in a protein conformational change: low-pH activation of the influenza virus hemagglutinin

At low pH, the hemagglutinin (HA) of influenza virus undergoes an irreversible conformational change that potentiates its essential membrane fusion function. We have probed the details of this conformational change using a panel of 14 anti-HA-peptide antibodies. Whereas some antibodies reacted equal...

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Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1987
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Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2114698/
https://www.ncbi.nlm.nih.gov/pubmed/2447101
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description At low pH, the hemagglutinin (HA) of influenza virus undergoes an irreversible conformational change that potentiates its essential membrane fusion function. We have probed the details of this conformational change using a panel of 14 anti-HA-peptide antibodies. Whereas some antibodies reacted equally well with both the neutral and low-pH HA conformations, others reacted to a significantly greater extent with the low-pH form. The locations of the peptides recognized by the latter antibodies in the three-dimensional HA structure indicated regions of the protein that change in response to low pH. Moreover, kinetic experiments suggested steps in the conformational change. In addition to their relevance to membrane fusion, our results show that anti-peptide antibodies can be used to study some types of biologically important protein conformational changes.
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spelling pubmed-21146982008-05-01 Anti-peptide antibodies detect steps in a protein conformational change: low-pH activation of the influenza virus hemagglutinin J Cell Biol Articles At low pH, the hemagglutinin (HA) of influenza virus undergoes an irreversible conformational change that potentiates its essential membrane fusion function. We have probed the details of this conformational change using a panel of 14 anti-HA-peptide antibodies. Whereas some antibodies reacted equally well with both the neutral and low-pH HA conformations, others reacted to a significantly greater extent with the low-pH form. The locations of the peptides recognized by the latter antibodies in the three-dimensional HA structure indicated regions of the protein that change in response to low pH. Moreover, kinetic experiments suggested steps in the conformational change. In addition to their relevance to membrane fusion, our results show that anti-peptide antibodies can be used to study some types of biologically important protein conformational changes. The Rockefeller University Press 1987-12-01 /pmc/articles/PMC2114698/ /pubmed/2447101 Text en This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/).
spellingShingle Articles
Anti-peptide antibodies detect steps in a protein conformational change: low-pH activation of the influenza virus hemagglutinin
title Anti-peptide antibodies detect steps in a protein conformational change: low-pH activation of the influenza virus hemagglutinin
title_full Anti-peptide antibodies detect steps in a protein conformational change: low-pH activation of the influenza virus hemagglutinin
title_fullStr Anti-peptide antibodies detect steps in a protein conformational change: low-pH activation of the influenza virus hemagglutinin
title_full_unstemmed Anti-peptide antibodies detect steps in a protein conformational change: low-pH activation of the influenza virus hemagglutinin
title_short Anti-peptide antibodies detect steps in a protein conformational change: low-pH activation of the influenza virus hemagglutinin
title_sort anti-peptide antibodies detect steps in a protein conformational change: low-ph activation of the influenza virus hemagglutinin
topic Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2114698/
https://www.ncbi.nlm.nih.gov/pubmed/2447101