title: Structural and functional similarity between Yersinia pestis capsular protein Caf1 and human interleukin-1 beta.
abstract: A comparative study of the structural and functional properties of recombinant Yersinia pestis Caf1 and human IL-1beta was performed. According to Fourier transform infrared spectroscopy (FTIR) and circular dichroism (CD) data, IL-1beta 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 (125)I-labeled IL-1beta to NIH 3T3 cells, and in the presence of Caf1, the binding of [(125)I]IL-1beta 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.
authors.affiliation: Institute of Immunological Engineering, 142380 Lyubuchany, Moscow Region, Russia.
authors.forename: V M
authors.initials: VM
authors.lastname: Abramov
authors.forename: A M
authors.initials: AM
authors.lastname: Vasiliev
authors.forename: R N
authors.initials: RN
authors.lastname: Vasilenko
authors.forename: N L
authors.initials: NL
authors.lastname: Kulikova
authors.forename: I V
authors.initials: IV
authors.lastname: Kosarev
authors.forename: V S
authors.initials: VS
authors.lastname: Khlebnikov
authors.forename: A T
authors.initials: AT
authors.lastname: Ishchenko
authors.forename: S
authors.initials: S
authors.lastname: MacIntyre
authors.forename: J R
authors.initials: JR
authors.lastname: Gillespie
authors.forename: R
authors.initials: R
authors.lastname: Khurana
authors.forename: T
authors.initials: T
authors.lastname: Korpela
authors.forename: A L
authors.initials: AL
authors.lastname: Fink
authors.forename: V N
authors.initials: VN
authors.lastname: Uversky
mesh_terms: D016475:3T3 Cells; D000817:Anilino Naphthalenesulfonates / Q000737:chemistry; D000818:Animals; D002850:Chromatography, Gel; D002942:Circular Dichroism; D005095:Exoribonucleases; D005347:Fibroblasts / Q000378:metabolism; D006801:Humans; D007375:Interleukin-1 / Q000737:chemistry* / Q000378:metabolism / Q000502:physiology*; D051379:Mice; D011485:Protein Binding; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D011506:Proteins; D012097:Repressor Proteins; D012260:Ribonucleases; D013050:Spectrometry, Fluorescence; D017550:Spectroscopy, Fourier Transform Infrared; D013329:Structure-Activity Relationship; D013816:Thermodynamics; D014157:Transcription Factors / Q000737:chemistry* / Q000378:metabolism / Q000502:physiology*; D014461:Ultracentrifugation; D015010:Yersinia pestis / Q000737:chemistry* / Q000502:physiology*
chemical_list: D000817:Anilino Naphthalenesulfonates; C489780:CNOT8 protein, human; D007375:Interleukin-1; D011506:Proteins; D012097:Repressor Proteins; D014157:Transcription Factors; C027132:1-anilino-8-naphthalenesulfonate; C489778:Cnot7 protein, mouse; D005095:Exoribonucleases; D012260:Ribonucleases