Virulence factor secretion and translocation by Bordetella species
نویسندگان
چکیده
منابع مشابه
Differential regulation of type III secretion and virulence genes in Bordetella pertussis and Bordetella bronchiseptica by a secreted anti-σ factor.
The BvgAS phosphorelay regulates ∼10% of the annotated genomes of Bordetella pertussis and Bordetella bronchiseptica and controls their infectious cycles. The hierarchical organization of the regulatory network allows the integration of contextual signals to control all or specific subsets of BvgAS-regulated genes. Here, we characterize a regulatory node involving a type III secretion system (T...
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Pertussis is still endemic and the recently resurgence of the disease caused by Bordetella pertussis has been shown in many countries. The polymorphism of the virulence genes of B. pertussis and lack of any information about the allelic variation between the Iranian isolates promotes us to analysis of the genes encoded virulence factors including ptxS1, prn, fim3 and cya to understand the diffe...
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The interaction between human neutrophils and wild-type Bordetella pertussis or mutants expressing altered lipopolysaccharide or lacking virulence factors-pertussis toxin, adenylate cyclase toxin, dermonecrotic toxin, filamentous hemagglutinin (FHA), pertactin, or BrkA-was examined. In the absence of antibodies, the wild-type strain and the mutants, with the exception of mutants lacking FHA, at...
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UNLABELLED Bordetella filamentous hemagglutinin (FHA), a primary component of acellular pertussis vaccines, contributes to virulence, but how it functions mechanistically is unclear. FHA is first synthesized as an ~370-kDa preproprotein called FhaB. Removal of an N-terminal signal peptide and a large C-terminal prodomain (PD) during secretion results in "mature" ~250-kDa FHA, which has been ass...
متن کاملSecretion of a bacterial virulence factor is driven by the folding of a C-terminal segment.
Autotransporters are bacterial virulence factors consisting of an N-terminal "passenger domain" that is secreted in a C- to-N-terminal direction and a C-terminal "β domain" that resides in the outer membrane (OM). Although passenger domain secretion does not appear to use ATP, the energy source for this reaction is unknown. Here, we show that efficient secretion of the passenger domain of the E...
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ژورنال
عنوان ژورنال: Current Opinion in Microbiology
سال: 2009
ISSN: 1369-5274
DOI: 10.1016/j.mib.2009.01.001