Molecular modeling of the steric structure of the envelope F1 antigen of Yersinia pestis

Immunology Letters
V P Zav'yalovT Korpela

Abstract

Steric structure of the envelope F1 protein of Yersinia pestis was reconstructed by computer modeling taking into account structural similarities between F1 and interleukins (IL)-1 alpha, -beta, -ra and by using the known atomic coordinates for huIL-1 beta obtained by the X-ray crystallography. Of 18 hydrophobic positions forming a hydrophobic core in all the proteins studied with the IL-1-like conformation, 15 positions are occupied by hydrophobic residues in F1 protein as well. Of 8 homologous positions occupied by the amino acid residues of similar charge in all huIL-1 alpha, -beta, -ra, 5 positions are conserved in F1 antigen. The B-cell epitope accessible to antibodies in polymeric F1 is exposed as an hydrophilic loop at the surface opposite to the C-terminal sequence, forming a conserved binding site with periplasmic molecular chaperones.

References

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Citations

Jan 21, 2000·FEMS Immunology and Medical Microbiology·L Sabhnani, D N Rao
Apr 3, 2001·Applied and Environmental Microbiology·A V ZavialovV P Zav'yalov
Feb 21, 2002·Infection and Immunity·Yidong DuAke Forsberg
Feb 20, 2014·International Journal of Nanomedicine·Shih-shiung HuangMing-kung Yeh
Aug 24, 2013·International Journal of Molecular Sciences·Marja T PöllänenRiikka Ihalin
Sep 27, 2005·Microbes and Infection·Dongsheng ZhouRuifu Yang
Oct 21, 1999·The Journal of Pharmacy and Pharmacology·I D SpiersE D Williamson
Oct 13, 2006·Journal of Medical Microbiology·Andrey P Anisimov, Kingsley K Amoako
Jan 1, 1997·Clinical Microbiology Reviews·R D Perry, J D Fetherston

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