In Silico and In Vitro Mutageneze lektinu PA-IIL - Korelace se strukturně-funkční analýzou

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14310%2F08%3A00025133" target="_blank" >RIV/00216224:14310/08:00025133 - isvavai.cz</a>

Výsledek na webu

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DOI - Digital Object Identifier

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Jazyk výsledku

angličtina

Název v původním jazyce

In Silico and In Vitro Mutagenesis of PA-IIL Lectin - Correlation with Structure-Function Analysis

Popis výsledku v původním jazyce

Protein-carbohydrate interactions play a crucial role in recognition and adhesion of pathogen to host tissue cells in the first step of their invasion and infectivity. Pseudomonas aeruginosa is an opportunistic pathogen, responsible for numerous nosocomial infections in immunocompromised patients. The bacterium colonises patients with chronic lung diseases and its infections is fatal in cystic fibrosis patients. P. aeruginosa produces a fucose-binding lectin PA-IIL that plays a role in virulence and adhesion [1]. Similar lectins have been found in other opportunistic bacteria like Ralstonia solanacearum [2], Chromobacterium violaceaum [3] and Burkholderia cenocepacia [4], with different binding preferences despite only slight sequence changes. Mutations of the PA-IIL lectin were designed according to these differences, cloned/modelled and investigated both in vitro, and in silico [5,6]. Thermodynamics of binding using isothermal titration microcalorimetry helped to rationalise importan

Název v anglickém jazyce

In Silico and In Vitro Mutagenesis of PA-IIL Lectin - Correlation with Structure-Function Analysis

Popis výsledku anglicky

Protein-carbohydrate interactions play a crucial role in recognition and adhesion of pathogen to host tissue cells in the first step of their invasion and infectivity. Pseudomonas aeruginosa is an opportunistic pathogen, responsible for numerous nosocomial infections in immunocompromised patients. The bacterium colonises patients with chronic lung diseases and its infections is fatal in cystic fibrosis patients. P. aeruginosa produces a fucose-binding lectin PA-IIL that plays a role in virulence and adhesion [1]. Similar lectins have been found in other opportunistic bacteria like Ralstonia solanacearum [2], Chromobacterium violaceaum [3] and Burkholderia cenocepacia [4], with different binding preferences despite only slight sequence changes. Mutations of the PA-IIL lectin were designed according to these differences, cloned/modelled and investigated both in vitro, and in silico [5,6]. Thermodynamics of binding using isothermal titration microcalorimetry helped to rationalise importan

Druh

D - Stať ve sborníku

CEP obor

BO - Biofyzika

OECD FORD obor

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Projekt

<a href="/cs/project/GA303%2F06%2F0570" target="_blank" >GA303/06/0570: Strukturně-funkční studie lektinů a adhezinů patogenních mikroorganismů</a><br>

Návaznosti

Z - Vyzkumny zamer (s odkazem do CEZ)

Rok uplatnění

2008

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název statě ve sborníku

Proceedings of the Eighth Triennial Congress of the World Association of Theoretical and Computational Chemists (WATOC 2008)

ISBN

978-0-646-50151-2

ISSN

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e-ISSN

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Počet stran výsledku

1

Strana od-do

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Název nakladatele

World Association of Theoretical and Computational Chemists

Místo vydání

Sydney

Místo konání akce

Sydney

Datum konání akce

1. 1. 2008

Typ akce podle státní příslušnosti

WRD - Celosvětová akce

Kód UT WoS článku

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