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Specific high affinity binding of human interleukin 1β by Caf1A usher protein of Yersinia pestis
Author(s) -
Zav'yalov Vladimir P.,
Chernovskaya Tatiana V.,
Navolotskaya Elena V.,
Karlyshev Andrey V.,
MacIntyre Sheila,
Vasiliev Anatoly M.,
Abramov Vyacheslav M.
Publication year - 1995
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(95)00878-d
Subject(s) - yersinia pestis , bacterial outer membrane , operon , yersinia , microbiology and biotechnology , biology , protein subunit , yersinia enterocolitica , bacteria , escherichia coli , virulence , biochemistry , gene , genetics
Understanding the interaction of Yersinia pestis with the key components of the immune system is important for elucidation of the pathogenesis of bubonic plague, one of the most severe and acute bacterial diseases. Here we report the specific, high affinity binding ( K d = 1.40 × 10 −10 M ± 0.14 × 10 −10 ) of radiolabelled human interleukin 1β (hIL‐1β) to E . coli cells carrying the capsular fl operon of Y. pestis. Caf1A outer membrane usher protein was isolated to greater than 98% purity. Competition studies with purified Caf1, together with immunoblotting studies, identified Caf1A as the hIL‐1β receptor. Competition between Caf1 subunit and hIL‐1β for the same or an overlapping binding site on CaflA was demonstrated. Relevance of these results to the pathogenesis of Y. pestis and other Gram negative bacterial pathogens with homologous outer membrane usher proteins is discussed.