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...
| Main Authors: | , , , , , |
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| Format: | Article |
| Language: | English |
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Taylor & Francis Group
2019-01-01
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| Series: | Journal of Oral Microbiology |
| Subjects: | |
| Online Access: | http://dx.doi.org/10.1080/20002297.2018.1565043 |
| _version_ | 1818039795052445696 |
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| author | Matthew L. Brewer David Dymock R. Leo Brady Bernhard B. Singer Mumtaz Virji Darryl J. Hill |
| author_facet | Matthew L. Brewer David Dymock R. Leo Brady Bernhard B. Singer Mumtaz Virji Darryl J. Hill |
| author_sort | Matthew L. Brewer |
| collection | DOAJ |
| 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. |
| first_indexed | 2024-12-10T08:04:18Z |
| format | Article |
| id | doaj.art-7f49ede41c7144dab76ae536caa2eb74 |
| institution | Directory Open Access Journal |
| issn | 2000-2297 |
| language | English |
| last_indexed | 2024-12-10T08:04:18Z |
| publishDate | 2019-01-01 |
| publisher | Taylor & Francis Group |
| record_format | Article |
| series | Journal of Oral Microbiology |
| spelling | doaj.art-7f49ede41c7144dab76ae536caa2eb742022-12-22T01:56:43ZengTaylor & Francis GroupJournal of Oral Microbiology2000-22972019-01-0111110.1080/20002297.2018.15650431565043Fusobacterium spp. target human CEACAM1 via the trimeric autotransporter adhesin CbpFMatthew L. Brewer0David Dymock1R. Leo Brady2Bernhard B. Singer3Mumtaz Virji4Darryl J. Hill5University of BristolUniversity of BristolUniversity of BristolUniversitätsklinikum EssenUniversity of BristolUniversity of BristolNeisseria 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.http://dx.doi.org/10.1080/20002297.2018.1565043fusobacteriumceacam1ceahost–pathogen interactionadhesionbindingtrimeric autotransporter adhesintaatype v secretionfusobacterium nucleatum |
| spellingShingle | Matthew L. Brewer David Dymock R. Leo Brady Bernhard B. Singer Mumtaz Virji Darryl J. Hill Fusobacterium spp. target human CEACAM1 via the trimeric autotransporter adhesin CbpF Journal of Oral Microbiology fusobacterium ceacam1 cea host–pathogen interaction adhesion binding trimeric autotransporter adhesin taa type v secretion fusobacterium nucleatum |
| 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 | fusobacterium ceacam1 cea host–pathogen interaction adhesion binding trimeric autotransporter adhesin taa type v secretion fusobacterium nucleatum |
| url | http://dx.doi.org/10.1080/20002297.2018.1565043 |
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