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Antibody against Microbial Neuraminidases Recognizes Human Sialidase 3 (NEU3): the Neuraminidase/Sialidase Superfamily Revisited

Neuraminidases (NAs) are critical virulence factors for several microbial pathogens. With a highly conserved catalytic domain, a microbial NA “superfamily” has been proposed. We previously reported that murine polymorphonuclear leukocyte (PMN) sialidase activity was important in leukocyte traffickin...

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Autores principales: Feng, Chiguang, Li, Jihong, Snyder, Greg, Huang, Wei, Goldblum, Simeon E., Chen, Wilbur H., Wang, Lai-Xi, McClane, Bruce A., Cross, Alan S.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Society for Microbiology 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5487728/
https://www.ncbi.nlm.nih.gov/pubmed/28655817
http://dx.doi.org/10.1128/mBio.00078-17
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author Feng, Chiguang
Li, Jihong
Snyder, Greg
Huang, Wei
Goldblum, Simeon E.
Chen, Wilbur H.
Wang, Lai-Xi
McClane, Bruce A.
Cross, Alan S.
author_facet Feng, Chiguang
Li, Jihong
Snyder, Greg
Huang, Wei
Goldblum, Simeon E.
Chen, Wilbur H.
Wang, Lai-Xi
McClane, Bruce A.
Cross, Alan S.
author_sort Feng, Chiguang
collection PubMed
description Neuraminidases (NAs) are critical virulence factors for several microbial pathogens. With a highly conserved catalytic domain, a microbial NA “superfamily” has been proposed. We previously reported that murine polymorphonuclear leukocyte (PMN) sialidase activity was important in leukocyte trafficking to inflamed sites and that antibodies to Clostridium perfringens NA recognized a cell surface molecule(s), presumed to be a sialidase of eukaryotic origin on interleukin-8-stimulated human and murine PMNs. These antibodies also inhibited cell sialidase activity both in vitro and, in the latter instance, in vivo. We therefore hypothesized that mammalian sialidases share structural homology and epitopes with microbial NAs. We now report that antibodies to one of the isoforms of C. perfringens NA, as well as anti-influenza virus NA serum, recognize human NEU3 but not NEU1 and that antibodies to C. perfringens NA inhibit NEU3 enzymatic activity. We conclude that the previously described microbial NA superfamily extends to human sialidases. Strategies designed to therapeutically inhibit microbial NA may need to consider potential compromising effects on human sialidases, particularly those expressed in cells of the immune system.
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spelling pubmed-54877282017-07-05 Antibody against Microbial Neuraminidases Recognizes Human Sialidase 3 (NEU3): the Neuraminidase/Sialidase Superfamily Revisited Feng, Chiguang Li, Jihong Snyder, Greg Huang, Wei Goldblum, Simeon E. Chen, Wilbur H. Wang, Lai-Xi McClane, Bruce A. Cross, Alan S. mBio Research Article Neuraminidases (NAs) are critical virulence factors for several microbial pathogens. With a highly conserved catalytic domain, a microbial NA “superfamily” has been proposed. We previously reported that murine polymorphonuclear leukocyte (PMN) sialidase activity was important in leukocyte trafficking to inflamed sites and that antibodies to Clostridium perfringens NA recognized a cell surface molecule(s), presumed to be a sialidase of eukaryotic origin on interleukin-8-stimulated human and murine PMNs. These antibodies also inhibited cell sialidase activity both in vitro and, in the latter instance, in vivo. We therefore hypothesized that mammalian sialidases share structural homology and epitopes with microbial NAs. We now report that antibodies to one of the isoforms of C. perfringens NA, as well as anti-influenza virus NA serum, recognize human NEU3 but not NEU1 and that antibodies to C. perfringens NA inhibit NEU3 enzymatic activity. We conclude that the previously described microbial NA superfamily extends to human sialidases. Strategies designed to therapeutically inhibit microbial NA may need to consider potential compromising effects on human sialidases, particularly those expressed in cells of the immune system. American Society for Microbiology 2017-06-27 /pmc/articles/PMC5487728/ /pubmed/28655817 http://dx.doi.org/10.1128/mBio.00078-17 Text en Copyright © 2017 Feng et al. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution 4.0 International license (http://creativecommons.org/licenses/by/4.0/) .
spellingShingle Research Article
Feng, Chiguang
Li, Jihong
Snyder, Greg
Huang, Wei
Goldblum, Simeon E.
Chen, Wilbur H.
Wang, Lai-Xi
McClane, Bruce A.
Cross, Alan S.
Antibody against Microbial Neuraminidases Recognizes Human Sialidase 3 (NEU3): the Neuraminidase/Sialidase Superfamily Revisited
title Antibody against Microbial Neuraminidases Recognizes Human Sialidase 3 (NEU3): the Neuraminidase/Sialidase Superfamily Revisited
title_full Antibody against Microbial Neuraminidases Recognizes Human Sialidase 3 (NEU3): the Neuraminidase/Sialidase Superfamily Revisited
title_fullStr Antibody against Microbial Neuraminidases Recognizes Human Sialidase 3 (NEU3): the Neuraminidase/Sialidase Superfamily Revisited
title_full_unstemmed Antibody against Microbial Neuraminidases Recognizes Human Sialidase 3 (NEU3): the Neuraminidase/Sialidase Superfamily Revisited
title_short Antibody against Microbial Neuraminidases Recognizes Human Sialidase 3 (NEU3): the Neuraminidase/Sialidase Superfamily Revisited
title_sort antibody against microbial neuraminidases recognizes human sialidase 3 (neu3): the neuraminidase/sialidase superfamily revisited
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5487728/
https://www.ncbi.nlm.nih.gov/pubmed/28655817
http://dx.doi.org/10.1128/mBio.00078-17
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