Heterologous expression of Bartonella adhesin A in Escherichia coli by exchange of trimeric autotransporter adhesin domains results in enhanced adhesion properties and a pathogenic phenotype.

ABSTRACT: Human-pathogenic Bartonella henselae causes cat scratch disease and vasculoproliferative disorders. An important pathogenicity factor of B. henselae is the trimeric autotransporter adhesin (TAA) Bartonella adhesin A (BadA), which is modularly constructed, consisting of a head, a long and repetitive neck-stalk module, and a membrane anchor. BadA is involved in bacterial autoagglutination, binding to extracellular matrix proteins and host cells, and in proangiogenic reprogramming. The slow growth of B. henselae and limited tools for genetic manipulation are obstacles for detailed examination of BadA and its domains. Here, we established a recombinant expression system for BadA mutants in Escherichia coli allowing functional analysis of particular BadA domains. Using a BadA mutant lacking 21

SUBMITTER: Schmidgen T 

PROVIDER: S-EPMC4054196 | biostudies-literature | 2014 Jun

REPOSITORIES: biostudies-literature