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Anthrax protective antigen is a calcium-dependent serine protease

Bacillus anthracis secretes a three component exotoxin-complex, which contributes to anthrax pathogenesis. Formation of this complex starts with the binding of protective antigen (PA) to its cellular receptor. In this study, we report that PA is a calcium-dependent serine protease and that the prote...

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Autores principales: Storm, Lisanne, Bikker, Floris J., Nazmi, Kamran, Hulst, Albert G., der Riet-Van Oeveren, Debora V., Veerman, Enno C.I., Hays, John P., Kaman, Wendy E.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Taylor & Francis 2018
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6086315/
https://www.ncbi.nlm.nih.gov/pubmed/30052476
http://dx.doi.org/10.1080/21505594.2018.1486139
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author Storm, Lisanne
Bikker, Floris J.
Nazmi, Kamran
Hulst, Albert G.
der Riet-Van Oeveren, Debora V.
Veerman, Enno C.I.
Hays, John P.
Kaman, Wendy E.
author_facet Storm, Lisanne
Bikker, Floris J.
Nazmi, Kamran
Hulst, Albert G.
der Riet-Van Oeveren, Debora V.
Veerman, Enno C.I.
Hays, John P.
Kaman, Wendy E.
author_sort Storm, Lisanne
collection PubMed
description Bacillus anthracis secretes a three component exotoxin-complex, which contributes to anthrax pathogenesis. Formation of this complex starts with the binding of protective antigen (PA) to its cellular receptor. In this study, we report that PA is a calcium-dependent serine protease and that the protein potentially uses this proteolytic activity for receptor binding. Additionally our findings shed new light on previous research describing the inhibition of anthrax toxins and exotoxin formation. Importantly, inhibition of the proteolytic activity of protective antigen could be a novel therapeutic strategy in fighting B. anthracis-related infections.
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spelling pubmed-60863152018-08-14 Anthrax protective antigen is a calcium-dependent serine protease Storm, Lisanne Bikker, Floris J. Nazmi, Kamran Hulst, Albert G. der Riet-Van Oeveren, Debora V. Veerman, Enno C.I. Hays, John P. Kaman, Wendy E. Virulence Brief Report Bacillus anthracis secretes a three component exotoxin-complex, which contributes to anthrax pathogenesis. Formation of this complex starts with the binding of protective antigen (PA) to its cellular receptor. In this study, we report that PA is a calcium-dependent serine protease and that the protein potentially uses this proteolytic activity for receptor binding. Additionally our findings shed new light on previous research describing the inhibition of anthrax toxins and exotoxin formation. Importantly, inhibition of the proteolytic activity of protective antigen could be a novel therapeutic strategy in fighting B. anthracis-related infections. Taylor & Francis 2018-07-27 /pmc/articles/PMC6086315/ /pubmed/30052476 http://dx.doi.org/10.1080/21505594.2018.1486139 Text en © 2018 The Author(s). Published by Informa UK Limited, trading as Taylor & Francis Group. http://creativecommons.org/licenses/by/4.0/ This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Brief Report
Storm, Lisanne
Bikker, Floris J.
Nazmi, Kamran
Hulst, Albert G.
der Riet-Van Oeveren, Debora V.
Veerman, Enno C.I.
Hays, John P.
Kaman, Wendy E.
Anthrax protective antigen is a calcium-dependent serine protease
title Anthrax protective antigen is a calcium-dependent serine protease
title_full Anthrax protective antigen is a calcium-dependent serine protease
title_fullStr Anthrax protective antigen is a calcium-dependent serine protease
title_full_unstemmed Anthrax protective antigen is a calcium-dependent serine protease
title_short Anthrax protective antigen is a calcium-dependent serine protease
title_sort anthrax protective antigen is a calcium-dependent serine protease
topic Brief Report
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6086315/
https://www.ncbi.nlm.nih.gov/pubmed/30052476
http://dx.doi.org/10.1080/21505594.2018.1486139
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