Structural and functional similarity between Yersinia pestis capsular protein Caf1 and human interleukin-1β

被引:18
|
作者
Abramov, VM
Vasiliev, AM
Vasilenko, RN
Kulikova, NL
Kosarev, IV
Khlebnikov, VS
Ishchenko, AT
MacIntyre, S
Gillespie, JR
Khurana, R
Korpela, T
Fink, AL
Uversky, VN [1 ]
机构
[1] Univ Calif Santa Cruz, Dept Chem & Biochem, Santa Cruz, CA 95064 USA
[2] Inst Immunol Engn, Lyubuchany 142380, Moscow Region, Russia
[3] Univ Reading, Sch Anim & Microbial Sci, Div Microbiol, Reading RG6 6AJ, Berks, England
[4] Univ Turku, Finnish Russian Joint Biotechnol Lab, Dept Biochem, SF-20520 Turku, Finland
[5] Russian Acad Sci, Inst Biol Instrumentat, Pushchino 142292, Moscow Region, Russia
关键词
D O I
10.1021/bi002678x
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
A comparative study of the structural and functional properties of recombinant Yersinia pestis Caf1 and human IL-1 beta was performed. According to Fourier transform infrared spectroscopy (FTIR) and circular dichroism (CD) data, IL-1 beta and Caf1 are typical beta -structural proteins. Neither protein interacts with the hydrophobic probe ANS (8-anilino-1-naphthalenesulfonate) under physiological conditions. Specific binding of Caf1 [K-d (5.4 +/- 0.1) x 10(-10) M] to interleukin-1 receptors (IL-1Rs) on the surface of finite mouse fibroblasts (line NIH 3T3) was observed. Caf1 is able to inhibit high-affinity binding of I-125- labeled IL-1 beta to NIH 3T3 cells, and in the presence of Caf1, the binding of [I-125]IL-1 beta is characterized by a K-d of (2.0 +/- 0.3) x 10(-9) M. Caf1 binding to IL-1R could reflect adhesive properties of the capsular subunits responsible for the contact of bacteria with the host immunocompetent cells. In its turn, this may represent a signal for the initiation of the expression and secretion of the proteins of Y, pestis Yop virulon. Thus, these results help to explain the importance of Caf1 in the interaction of Y. pestis with the host immune system.
引用
收藏
页码:6076 / 6084
页数:9
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