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Fusobacterium spp. target human CEACAM1 via the trimeric autotransporter adhesin CbpF

Neisseria meningitidis, Haemophilus influenzae, and Moraxella catarrhalis are pathogenic bacteria adapted to reside on human respiratory mucosal epithelia. One common feature of these species is their ability to target members of the carcinoembryonic antigen-related cell adhesion molecule (CEACAM) f...

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Autores principales: Brewer, Matthew L., Dymock, David, Brady, R. Leo, Singer, Bernhard B., Virji, Mumtaz, Hill, Darryl J.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Taylor & Francis 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6346709/
https://www.ncbi.nlm.nih.gov/pubmed/30719234
http://dx.doi.org/10.1080/20002297.2018.1565043
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author Brewer, Matthew L.
Dymock, David
Brady, R. Leo
Singer, Bernhard B.
Virji, Mumtaz
Hill, Darryl J.
author_facet Brewer, Matthew L.
Dymock, David
Brady, R. Leo
Singer, Bernhard B.
Virji, Mumtaz
Hill, Darryl J.
author_sort Brewer, Matthew L.
collection PubMed
description Neisseria meningitidis, Haemophilus influenzae, and Moraxella catarrhalis are pathogenic bacteria adapted to reside on human respiratory mucosal epithelia. One common feature of these species is their ability to target members of the carcinoembryonic antigen-related cell adhesion molecule (CEACAM) family, especially CEACAM1, which is achieved via structurally distinct ligands expressed by each species. Beside respiratory epithelial cells, cells at the dentogingival junction express high levels of CEACAM1. It is possible that bacterial species resident within the oral cavity also utilise CEACAM1 for colonisation and invasion of gingival tissues. From a screen of 59 isolates from the human oral cavity representing 49 bacterial species, we identified strains from Fusobacterium bound to CEACAM1. Of the Fusobacterium species tested, the CEACAM1-binding property was exhibited by F. nucleatum (Fn) and F. vincentii (Fv) but not F. polymorphum (Fp) or F. animalis (Fa) strains tested. These studies identified that CEACAM adhesion was mediated using a trimeric autotransporter adhesin (TAA) for which no function has thus far been defined. We therefore propose the name CEACAM binding protein of Fusobacterium (CbpF). CbpF was identified to be present in the majority of unspeciated Fusobacterium isolates confirming a subset of Fusobacterium spp. are able to target human CEACAM1.
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spelling pubmed-63467092019-02-04 Fusobacterium spp. target human CEACAM1 via the trimeric autotransporter adhesin CbpF Brewer, Matthew L. Dymock, David Brady, R. Leo Singer, Bernhard B. Virji, Mumtaz Hill, Darryl J. J Oral Microbiol Original Article Neisseria meningitidis, Haemophilus influenzae, and Moraxella catarrhalis are pathogenic bacteria adapted to reside on human respiratory mucosal epithelia. One common feature of these species is their ability to target members of the carcinoembryonic antigen-related cell adhesion molecule (CEACAM) family, especially CEACAM1, which is achieved via structurally distinct ligands expressed by each species. Beside respiratory epithelial cells, cells at the dentogingival junction express high levels of CEACAM1. It is possible that bacterial species resident within the oral cavity also utilise CEACAM1 for colonisation and invasion of gingival tissues. From a screen of 59 isolates from the human oral cavity representing 49 bacterial species, we identified strains from Fusobacterium bound to CEACAM1. Of the Fusobacterium species tested, the CEACAM1-binding property was exhibited by F. nucleatum (Fn) and F. vincentii (Fv) but not F. polymorphum (Fp) or F. animalis (Fa) strains tested. These studies identified that CEACAM adhesion was mediated using a trimeric autotransporter adhesin (TAA) for which no function has thus far been defined. We therefore propose the name CEACAM binding protein of Fusobacterium (CbpF). CbpF was identified to be present in the majority of unspeciated Fusobacterium isolates confirming a subset of Fusobacterium spp. are able to target human CEACAM1. Taylor & Francis 2019-01-24 /pmc/articles/PMC6346709/ /pubmed/30719234 http://dx.doi.org/10.1080/20002297.2018.1565043 Text en © 2019 University of Bristol. 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 Original Article
Brewer, Matthew L.
Dymock, David
Brady, R. Leo
Singer, Bernhard B.
Virji, Mumtaz
Hill, Darryl J.
Fusobacterium spp. target human CEACAM1 via the trimeric autotransporter adhesin CbpF
title Fusobacterium spp. target human CEACAM1 via the trimeric autotransporter adhesin CbpF
title_full Fusobacterium spp. target human CEACAM1 via the trimeric autotransporter adhesin CbpF
title_fullStr Fusobacterium spp. target human CEACAM1 via the trimeric autotransporter adhesin CbpF
title_full_unstemmed Fusobacterium spp. target human CEACAM1 via the trimeric autotransporter adhesin CbpF
title_short Fusobacterium spp. target human CEACAM1 via the trimeric autotransporter adhesin CbpF
title_sort fusobacterium spp. target human ceacam1 via the trimeric autotransporter adhesin cbpf
topic Original Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6346709/
https://www.ncbi.nlm.nih.gov/pubmed/30719234
http://dx.doi.org/10.1080/20002297.2018.1565043
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