Abstract
ABSTRACTNeisseria 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.
Highlights
The overall consensus strength is shown by coloured histograms above each aligned amino acid; increasing height and colour indicates increased consensus strength
ID NumberF. sp. F. sp. F. sp. F. sp. F. sp. F. sp. F. sp. F. sp. F. sp. F. sp. F. sp. F. sp. F. sp. F. sp. F. sp. F. sp. F. sp. F. sp. F. sp. F. sp. F. sp. F. sp. F. sp. F. sp. F. sp. F. sp. F. sp. F. sp. F. nucleatum F. nucleatum F sp. F. sp. F. vincentiii (formerly F. nucleatum sp. Fusiforme) F. sp. F sp. F. periodonticum
Summary
AFGINNTADGENSSAFGFKNKISGKWSSAFGNQYEVTGEKSGTFGVGEYN - GQYKYKNEGNNSYMIGNYN Fn 2B2.pro 140 AFGINNTASGEGSSAFGYINKVSGANSSVLGNQYEVTGNSSGAFGVGFWNSGSHLYKNEGNNSYMIGNKN Fn 2B3.pro 140 AFGINNTADGENSSAFGFKNKISGKWSSAFGNQYEVTGEKSGTFGVGEYN - GQYKYKNEGNNSYMIGNYN Fn 2B4.pro 140 AFGINNTASGEGSSAFGYINKVSGANSSVLGNQYEVTGNSSGAFGVGFWNSGSHLYKNEGNNSYMIGNKN Fn 2B8.pro 140 AFGINNTADGENSSAFGFKNKISGKWSSAFGNQYEVTGEKSGTFGVGEYN - GQYKYKNEGNNSYMIGNYN Fn 2B9.pro 56 AFGTGNKADGEDSSAFGSLNIASGKFSSAFGSQYEVTGNSSGAFGVGEFN - GSYQYKNEGNNSYMIGNKN Fn 2B13.pro 140 AFGINNTADGENSSAFGFKNIVSGFNSSAFGSQYEVTGNFSGAFGMGEFN - GQYQYKNEGNNSYMIGNKN Fn 2B16.pro 56 AFGTGNKADGEDSSAFGSLNIASGKFSSAFGSQYEVTGNSSGAFGVGEFN - GSYQYKNEGNNSYMIGNKN Fn 2B17.pro 56 AFGTGNKADGEDSSAFGSLNIASGKFSSAFGSQYEVTGNSSGAFGVGEYN - GSYQYKNEGNNSYMIGNKN Fn 2B32.pro 71 AFGSNNAADGVNSSAFGFKNTVSGFNSSAFGSQYQVTGNFSGAFGMGEFN - GQYQYKNEGNNSYMIGNKN Fnn.pro 56 AFGTGNKADGEDSSAFGSLNIASGKFSSAFGSQYEVTGNSSGAFGVGEFN - GSYQYKNEGNNSYMIGNKN Fnv.pro
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