Structural and Functional Similarity between Yersinia pestis Capsular Protein Caf1 and Human Interleukin-1β
| Autor: | Sheila MacIntyre, Raisa N. Vasilenko, Alexander T. Ishchenko, Vladimir N. Uversky, and Anthony L. Fink, Igor V. Kosarev, Timo Kalevi Korpela, Vyacheslav M. Abramov, Ritu Khurana, Nataly L. Kulikova, Valentin S. Khlebnikov, Anatoly M. Vasiliev, Joel R. Gillespie |
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| Rok vydání: | 2001 |
| Předmět: |
Circular dichroism
Protein Conformation Yersinia pestis Repressor Plasma protein binding Biochemistry Anilino Naphthalenesulfonates Protein Structure Secondary 3T3 cells Mice Structure-Activity Relationship Ribonucleases Protein structure Spectroscopy Fourier Transform Infrared medicine Animals Humans Secretion Receptor biology Chemistry Circular Dichroism Proteins 3T3 Cells Fibroblasts biology.organism_classification Molecular biology Repressor Proteins Crystallography Spectrometry Fluorescence medicine.anatomical_structure Exoribonucleases Chromatography Gel Thermodynamics Ultracentrifugation Interleukin-1 Protein Binding Transcription Factors |
| Zdroj: | Biochemistry. 40:6076-6084 |
| ISSN: | 1520-4995 0006-2960 |
| DOI: | 10.1021/bi002678x |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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