Structural and Functional Properties of Yersinia pestis Caf1 Capsular Antigen and Their Possible Role in Fulminant Development of Primary Pneumonic Plague

Autor:	and Anthony L. Fink, Vyacheslav M. Abramov, Joel R. Gillespie, Alexander T. Ishchenko, Valentin S. Khlebnikov, Nataly L. Kulikova, Ian S. Millett, Anatoly M. Vasiliev, Vladimir N. Uversky, Raisa N. Vasilenko, Igor V. Kosarev
Rok vydání:	2002
Předmět:	Pneumonic plague Protein Denaturation Protein Conformation Yersinia pestis Plasma protein binding Biology Models Biological Biochemistry Cell Line Microbiology Protein structure Bacterial Proteins Antigen Spectroscopy Fourier Transform Infrared medicine Animals Humans Macrophage Receptor Bacterial Capsules Guanidine Antigens Bacterial Plague Circular Dichroism Macrophages Receptors Interleukin-1 Epithelial Cells General Chemistry Hydrogen-Ion Concentration biology.organism_classification medicine.disease Bacterial adhesin Dimerization Protein Binding
Zdroj:	Journal of Proteome Research. 1:307-315
ISSN:	1535-3907 1535-3893
DOI:	10.1021/pr025511u
Popis:	Yersinia pestis capsular antigen Caf1 is shown to be a beta-structural protein that in polymeric form possesses very high conformational stability. Different approaches show that a dimer is the minimal cooperative block of Caf1 adhesin. Caf1 dimer interacts effectively with IL-1 receptors of human macrophage and epithelial cells. The specificity of such interaction is confirmed by the inhibition of IL-1alpha binding by Caf1. The Caf1 role in pneumonic plague pathogenesis is discussed.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bc20b2ff405e630b5f583768bed61dd2 https://doi.org/10.1021/pr025511u Zobrazit plný text záznamu