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@proceedings{959885,
author = {Pokorná, Martina and Mrázková, Jana and Wimmerová, Michaela},
booktitle = {36th FEBS Congress},
keywords = {PA-IIL; PA-IL; Pseudomonas aeruginosa; mutagenesis},
language = {eng},
title = {Specificity and affinity modulation of PA-IIL lectin},
year = {2011}
}
TY - CONF
ID - 959885
AU - Pokorná, Martina - Mrázková, Jana - Wimmerová, Michaela
PY - 2011
TI - Specificity and affinity modulation of PA-IIL lectin
KW - PA-IIL
KW - PA-IL
KW - Pseudomonas aeruginosa
KW - mutagenesis
N2 - Pseudomonas aeruginosa is a clinically important pathogen, which is responsible for numerous nosocomial infections in immunocompromised patients. The bacterium colonises patients with chronic lung diseases and its infection is fatal in cystic fibrosis patients. P. aeruginosa produces high levels of D galactose and L-fucose binding lectins, PA-IL (LecA) and PA-IIL (LecB) respectively, which are associated with its cytotoxic virulence and could be involved in primary recognition of the host organism and in biofilm formation.Additional experiments have been performed to order to understand the molecular basis of both specificity and affinity of PA-IIL for monosaccharides. Three single point mutants in position 22-23-24 have prepared and structure-functioned characterized. The mutated amino acids belong to the “specificity-binding loop”. The in vitro mutagenesis in combination with computational methods allowed the key importance of amino acid 22 for the specificity of the lectin to be identified.
ER -
POKORNÁ, Martina, Jana MRÁZKOVÁ a Michaela WIMMEROVÁ. Specificity and affinity modulation of PA-IIL lectin. In \textit{36th FEBS Congress}. 2011. ISSN~1742-464X.
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