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Statements

Subject Item
n2:RIV%2F00216224%3A14740%2F11%3A00050179%21RIV12-GA0-14740___
rdf:type
skos:Concept n9:Vysledek
dcterms:description
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. 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.
dcterms:title
Specificity and affinity modulation of PA-IIL lectin Specificity and affinity modulation of PA-IIL lectin
skos:prefLabel
Specificity and affinity modulation of PA-IIL lectin Specificity and affinity modulation of PA-IIL lectin
skos:notation
RIV/00216224:14740/11:00050179!RIV12-GA0-14740___
n9:predkladatel
n10:orjk%3A14740
n3:aktivita
n12:P
n3:aktivity
P(GPP207/11/P185)
n3:dodaniDat
n15:2012
n3:domaciTvurceVysledku
n5:5522064 n5:5616697 n5:6666477
n3:druhVysledku
n4:O
n3:duvernostUdaju
n17:S
n3:entitaPredkladatele
n7:predkladatel
n3:idSjednocenehoVysledku
231287
n3:idVysledku
RIV/00216224:14740/11:00050179
n3:jazykVysledku
n18:eng
n3:klicovaSlova
PA-IIL; PA-IL; Pseudomonas aeruginosa; mutagenesis
n3:klicoveSlovo
n6:Pseudomonas%20aeruginosa n6:PA-IL n6:PA-IIL n6:mutagenesis
n3:kontrolniKodProRIV
[1144C054698F]
n3:obor
n14:CE
n3:pocetDomacichTvurcuVysledku
3
n3:pocetTvurcuVysledku
3
n3:projekt
n11:GPP207%2F11%2FP185
n3:rokUplatneniVysledku
n15:2011
n3:tvurceVysledku
Pokorná, Martina Mrázková, Jana Wimmerová, Michaela
n16:organizacniJednotka
14740