2012
DOI: 10.1111/cmi.12070
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Bartonella henselaetrimeric autotransporter adhesin BadA expression interferes with effector translocation by the VirB/D4 type IV secretion system

Abstract: SummaryThe Gram-negative, zoonotic pathogen Bartonella henselae is the aetiological agent of cat scratch disease, bacillary angiomatosis and peliosis hepatis in humans. Two pathogenicity factors of B. henselae -each displaying multiple functions in host cell interaction -have been characterized in greater detail: the trimeric autotransporter Bartonella adhesin A (BadA) and the type IV secretion system VirB/D4 (VirB/D4 T4SS). BadA mediates, e.g. binding to fibronectin (Fn), adherence to endothelial cells (ECs) … Show more

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Cited by 49 publications
(50 citation statements)
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“…Surprisingly, and in contrast to what occurs in Y. enterocolitica, where YadA enhances type III secretion of Yersinia outer proteins into host cells (34), injection of Bartonella effector proteins (Beps) into host cells by the B. henselae VirB/D4 type 4 secretion system is inhibited by BadA expression (17). However, it has to be emphasized that functional analysis of single BadA domains by orthologous expression in B. henselae is complicated by the limited number of genetic tools for construction of such mutants and the very slow growth of the pathogen (6).…”
Section: Discussionmentioning
confidence: 76%
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“…Surprisingly, and in contrast to what occurs in Y. enterocolitica, where YadA enhances type III secretion of Yersinia outer proteins into host cells (34), injection of Bartonella effector proteins (Beps) into host cells by the B. henselae VirB/D4 type 4 secretion system is inhibited by BadA expression (17). However, it has to be emphasized that functional analysis of single BadA domains by orthologous expression in B. henselae is complicated by the limited number of genetic tools for construction of such mutants and the very slow growth of the pathogen (6).…”
Section: Discussionmentioning
confidence: 76%
“…A crucial role of B. henselae BadA in the infection process of ECs was demonstrated (4), and the head domain of BadA turned out to be decisive for EC binding (15). However, B. henselae harbors further potential adhesins in its genome, e.g., filamentous hemagglutinins (17,28), which might interact with this process. Therefore, we investigated BadA-mediated adherence to ECs using E. coli expressing BadA HN23 hybrid 3.…”
Section: Resultsmentioning
confidence: 99%
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“…TAA-dependent adherence of B. henselae and A. baumannii. Since the role of BadA in mediating bacterial adherence to ECs has been analyzed in detail (2,5,6,32,33), B. henselae was used in our study as a control to calibrate the experiments with A. baumannii. Previous works described mainly Ata-dependent adhesion abilities of A. baumannii to ECMs under static infection conditions (3).…”
Section: Discussionmentioning
confidence: 99%
“…Bartonella TAAs additionally induce angiogenesis and serum resistance (O'Rourke et al 2011). Interestingly, BadA expression on the bacterial surface masks the activity of the VirB T4SS (Lu et al 2013), but these two major virulence factors are differentially regulated on the transcriptional level via the TC system BatS/ BatR, indicating that the two act at different stages of the infection process.…”
Section: Adhesion Molecules: Key For Host -Pathogen Interactionmentioning
confidence: 99%