Abstract
The homologues LcrV of Yersinia species and PcrV of Pseudomonas aeruginosa are pore-forming components. When expressed in a Yersinia lcrV background, PcrV formed smaller pores in infected erythrocyte membranes, correlating to a lowered translocation of Yersinia effectors. To understand this phenomenon, cytotoxins exoenzyme S of P. aeruginosa and YopE of Yersinia were introduced into a Yersinia background without Yop effectors but expressing LcrV or PcrV. Comparable translocation of each substrate indicated that substrate recognition by LcrV/PcrV is not a regulator of translocation. Yersinia harboring pcrV coexpressed with its native operon efficiently translocated effectors into HeLa cell monolayers and formed large LcrV-like pores in erythrocyte membranes. Thus, a PcrV complex with native P. aeruginosa translocon components is required to form fully functional pores for complete complementation of effector translocation in Yersinia.
Publication types
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Comparative Study
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Research Support, Non-U.S. Gov't
MeSH terms
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Antigens, Bacterial / genetics
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Antigens, Bacterial / metabolism*
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Bacterial Outer Membrane Proteins / genetics
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Bacterial Outer Membrane Proteins / metabolism
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Bacterial Toxins / genetics
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Bacterial Toxins / metabolism*
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Erythrocyte Membrane / metabolism
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Erythrocyte Membrane / microbiology
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Gene Deletion
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Gene Expression
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Genetic Complementation Test
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HeLa Cells
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Histidine Kinase
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Humans
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Operon / genetics
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Phenotype
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Pore Forming Cytotoxic Proteins
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Protein Kinases / genetics
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Protein Kinases / metabolism
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Protein Transport
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Pseudomonas aeruginosa / genetics*
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Substrate Specificity
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Yersinia pseudotuberculosis / genetics*
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Yersinia pseudotuberculosis / metabolism*
Substances
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Antigens, Bacterial
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Bacterial Outer Membrane Proteins
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Bacterial Toxins
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LcrV protein, Yersinia
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Pore Forming Cytotoxic Proteins
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antigen V, Pseudomonas
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yopE protein, Yersinia
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Protein Kinases
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Histidine Kinase