The Complete Genome Sequence of the Fish Pathogen Tenacibaculum maritimum Provides Insights into Virulence Mechanisms
Type | Article | ||||||||||||||||||||||||||||||||||||
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Date | 2017-08 | ||||||||||||||||||||||||||||||||||||
Language | English | ||||||||||||||||||||||||||||||||||||
Author(s) | Perez-Pascual David![]() ![]() |
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Affiliation(s) | 1 : Univ Paris Saclay, INRA, Virol & Immunol Mol, Jouy En Josas, France. 2 : Genoscope, Inst Genom, Commissiariat Energie Atom & Energies Alternat, Evry, France. 3 : Genoscope, Inst Genom, Commissariat Energie Atom & Energies Alternat, CNRS,UMR 8030,Lab Anal Bioinformat Genom & Met, Evry, France. 4 : INRA, Genotoul Genome & Transcriptome GeT PlaGe, Castanet Tolosan, France. 5 : INRA, UAR1209, Castanet Tolosan, France. 6 : Sorbonne Univ, Stn Biol Roscoff, Univ Pierre & Marie Curie, CNRS,UMR 8227,Lab Biol Integrat Modeles Marins, Roscoff, France. |
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Source | Frontiers In Microbiology (1664-302X) (Frontiers Media Sa), 2017-08 , Vol. 8 , N. 1542 , P. 11p. | ||||||||||||||||||||||||||||||||||||
DOI | 10.3389/fmicb.2017.01542 | ||||||||||||||||||||||||||||||||||||
WOS© Times Cited | 42 | ||||||||||||||||||||||||||||||||||||
Keyword(s) | Tenacibaculum maritimum, fish pathogen, virulence factors, genome, toxins | ||||||||||||||||||||||||||||||||||||
Abstract | Tenacibaculum maritimum is a devastating bacterial pathogen of wild and farmed marine fish with a broad host range and a worldwide distribution. We report here the complete genome sequence of the T. maritimum type strain NCIMB 2154(T). The genome consists of a 3,435,971-base pair circular chromosome with 2,866 predicted protein-coding genes. Genes encoding the biosynthesis of exopolysaccharides, the type IX secretion system, iron uptake systems, adhesins, hemolysins, proteases, and glycoside hydrolases were identified. They are likely involved in the virulence process including immune escape, invasion, colonization, destruction of host tissues, and nutrient scavenging. Among the predicted virulence factors, type IX secretion-mediated and cell-surface exposed proteins were identified including an atypical sialidase, a sphingomyelinase and a chondroitin AC lyase which activities were demonstrated in vitro. | ||||||||||||||||||||||||||||||||||||
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