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Characterization of a Bvg-regulated fatty acid methyl-transferase in Bordetella pertussis

The whooping cough agent Bordetella pertussis controls the expression of its large virulence regulon in a coordinated manner through the two-component signal transduction system BvgAS. In addition to the genes coding for bona fide virulence factors, the Bvg regulon comprises genes of unknown functio...

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Detalles Bibliográficos
Autores principales: Rivera-Millot, Alex, Lesne, Elodie, Solans, Luis, Coutte, Loic, Bertrand-Michel, Justine, Froguel, Philippe, Dhennin, Véronique, Hot, David, Locht, Camille, Antoine, Rudy, Jacob-Dubuisson, Françoise
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5426589/
https://www.ncbi.nlm.nih.gov/pubmed/28493897
http://dx.doi.org/10.1371/journal.pone.0176396
Descripción
Sumario:The whooping cough agent Bordetella pertussis controls the expression of its large virulence regulon in a coordinated manner through the two-component signal transduction system BvgAS. In addition to the genes coding for bona fide virulence factors, the Bvg regulon comprises genes of unknown function. In this work, we characterized a new Bvg-activated gene called BP2936. Homologs of BP2936 are found in other pathogenic Bordetellae and in several other species, including plant pathogens and environmental bacteria. We showed that the gene product of BP2936 is a membrane-associated methyl-transferase of free fatty acids. We thus propose to name it FmtB, for fatty acid methyl-transferase of Bordetella. The role of this protein was tested in cellular and animal models of infection, but the loss of BP2936 did not appear to affect host-pathogen interactions in those assays. The high level of conservation of BP2936 among B. pertussis isolates nevertheless argues that it probably plays a role in the life cycle of this pathogen.