Failure to detect binding of LcrH to the V antigen of Yersinia pestis.
V antigen of Yersinia pestis has been reported to bind the chaperone LcrH. We were unable to demonstrate this interaction. Despite methodological differences between our study and an earlier study, we believe that the previous findings were artifactual. One likely confounding element was the tendency of LcrH to adhere on its own to metal chelation chromatographic resin.
Fields
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KA
Department of Microbiology and Immunology, Chandler Medical Center, University of Kentucky, Lexington 40536-0084, USA.
Williams
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AW
Straley
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SC
D000907:Antibodies, Bacterial / Q000276:immunology; D000942:Antigens, Bacterial / Q000378:metabolism*; D001426:Bacterial Proteins / Q000378:metabolism; D018832:Molecular Chaperones / Q000378:metabolism*; D009532:Nickel; D052899:Pore Forming Cytotoxic Proteins; D011233:Precipitin Tests; D011485:Protein Binding; D015010:Yersinia pestis / Q000737:chemistry*
D000907:Antibodies, Bacterial; D000942:Antigens, Bacterial; D001426:Bacterial Proteins; C043908:LcrV protein, Yersinia; D018832:Molecular Chaperones; D052899:Pore Forming Cytotoxic Proteins; D009532:Nickel