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@proceedings{1077984,
author = {Mrázková, Jana and Pokorná, Martina and Dejmková, Eva and Malinovská, Lenka and Wimmerová, Michaela},
booktitle = {XXIII. Biochemický sjezd},
keywords = {lectins; pathogenic bacteria; PA-IIL; Pseudomonas aeruginosa; RS-IIL; Ralstonia solanacearum; BC2L-A; Burkholderia cenocepacia; CV-IIL; Chromobacterium violaceum; site-directed mutagenesis; specificity; affinity; sugar binding},
language = {eng},
isbn = {978-80-86313-34-4},
title = {Influence of targeted amino acid substitution on specificity and affinity of lectins from pathogenic bacteria},
year = {2012}
}
TY - CONF
ID - 1077984
AU - Mrázková, Jana - Pokorná, Martina - Dejmková, Eva - Malinovská, Lenka - Wimmerová, Michaela
PY - 2012
TI - Influence of targeted amino acid substitution on specificity and affinity of lectins from pathogenic bacteria
SN - 9788086313344
KW - lectins
KW - pathogenic bacteria
KW - PA-IIL
KW - Pseudomonas aeruginosa
KW - RS-IIL
KW - Ralstonia solanacearum
KW - BC2L-A
KW - Burkholderia cenocepacia
KW - CV-IIL
KW - Chromobacterium violaceum
KW - site-directed mutagenesis
KW - specificity
KW - affinity
KW - sugar binding
N2 - Pseudomonas aeruginosa, Chromobacterium violaceum, Burkholderia cenocepacia and Ralstonia solanacearum are saprophytic bacteria found in various environments, including soil, water and vegetation. The first three bacteria occasionally become aggressive opportunistic animal and human pathogens which attack mainly immunocompromised patients, e.g. patients suffering from cystic fibrosis. The fourth bacterium is economically important plant pathogen. All these bacteria produce lectins. Lectins are proteins which are capable of binding diverse carbohydrates with varying specificity. This fact is very important especially in host-pathogen interactions, where lectins help pathogen in adhesion to sugar moieties presented on host cells. Foregoing bacteria produce lectins belonging to a so-called “PA-IIL family”, namely PA-IIL (P. aeruginosa), CV-IIL (C. violaceum), BC2L-A (B. cenocepacia) and RS-IIL (R. solanacearum). These lectins are orthologues with significant sequential and structural similarities. Although they bind similar saccharides, they differ in preferences towards these saccharides. RS-IIL and BC2L-A prefer D-mannose, while PA-IIL and CV-IIL prefer L-fucose. The aim of this work was preparation of mutated variants of these lectins with the amino acid substitution corresponding to the position Thr98 (in PA-IIL), which participates on sugar binding. Changes in affinities/ specificities of the mutants were measured by sothermal titration calorimetry (ITC) and surface plasmon resonance (SPR).
ER -
MRÁZKOVÁ, Jana, Martina POKORNÁ, Eva DEJMKOVÁ, Lenka MALINOVSKÁ and Michaela WIMMEROVÁ. Influence of targeted amino acid substitution on specificity and affinity of lectins from pathogenic bacteria. In \textit{XXIII. Biochemický sjezd}. 2012. ISBN~978-80-86313-34-4.
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