Destabilization of phospholipid model membranes by YplA, a phospholipase A2 secreted by Yersinia enterocolitica

Berring, Erin; Brancato, Sam J.; Grant, Katharine; Schaper, Elizabeth; Kadavil, Sheena; Smagin, Helen; Hatic, Safet O.; Picking, William D.; Serfis, Alexa Barnoski

doi:10.1016/j.chemphyslip.2004.04.009

Cited by 3 publications

(2 citation statements)

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“…2). The Y. enterocolitica YplA enzyme is an A2 phospholipase and is secreted under flagellar T3SS inducing conditions in Identification of C. jejuni CiaC 651 vitro (Schmiel et al, 1998;Berring et al, 2004). Warren and Young (2005) determined that the YplA enzyme's T3S amino-terminal sequence is localized within the first 20 residues.…”

Section: Jejuni T3s Amino-terminal Sequences Promote Secretion Fromentioning

confidence: 99%

“…Based on the finding that CiaB was secreted from Y. enterocolitica, we developed a screen that utilized Y. enterocolitica and the YplA effector protein to identify C. jejuni genes that encode amino-terminal residues that facilitate protein secretion in a T3SS-dependant manner (i.e. T3S amino-terminal sequences) (Schmiel et al ., 2000; Berring et al ., 2004; Warren and Young, 2005). We demonstrated that the screen had the potential to identify putative Csp with T3S amino-terminal sequences using known C. jejuni flagellar secreted proteins.…”

Section: Introductionmentioning

confidence: 99%

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Identification of a Campylobacter jejuni‐secreted protein required for maximal invasion of host cells

Christensen

Pacheco

Konkel³

2009

Molecular Microbiology

113

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The food-borne pathogen Campylobacter jejuni is dependent on a functional flagellum for motility and the export of virulence proteins that promote maximal host cell invasion. Both the flagellar and non-flagellar proteins exported via the flagellar type III secretion system contain a sequence within the amino-terminus that directs their export from the bacterial cell. Accordingly, we developed a genetic screen to identify C. jejuni genes that encode a type III secretion amino-terminal sequence that utilizes the flagellar type III secretion system of Yersinia enterocolitica and a phospholipase reporter (yplA). We screened a library of 321 C. jejuni genes and identified proteins with putative type III secretion amino-terminal sequences. One gene identified by the screen was Cj1242. We generated a mutation in Cj1242, and performed growth rate, motility, secretion and INT 407 cell adherence and internalization assays. The C. jejuni Cj1242 mutant was not altered in growth rate or motility when compared with the wild-type strain, but displayed an altered secretion profile and a reduction in host cell internalization. Based on the phenotype of the C. jejuni Cj1242 mutant, we designated the protein Campylobacter invasion antigen C (CiaC). Collectively, our findings indicate that CiaC is a potentially important virulence factor.

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Section: Jejuni T3s Amino-terminal Sequences Promote Secretion Fromentioning

confidence: 99%