Strukturně funkční charakterizace nového lektinu z bakterie Chromobacterium violaceum

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14310%2F05%3A00013840" target="_blank" >RIV/00216224:14310/05:00013840 - 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

Sructure-function characterisation of a new lectin from Chromobacterium violaceum

Popis výsledku v původním jazyce

Carbohydrates are essential components of life that play crucial role in all organisms. They are very important agent in recognition and signalling ways. Lectin-carbohydrate interactions play a crucial role in many recognition events. Pseudomonas aeruginosa, an opportunistic pathogen responsible for numerous nosocomial infections in immunocopromised patients, produces a variety of carbohydrate-binding proteins that could be involved in host recognition and adhesion. One of them, PA-IIL, is a fucose binding lectin that is closely related to the virulence of the bacterium [1]. Searching in databases for proteins displaying sequence similarities to PA-IIL revealed new homologous proteins in other opportunistic pathogens like Chromobacterium violaceum. Human infection by Ch. violaceum is rare but when it occurs, it is associated with very high mortality rate [2]. In Ch. violaceum genome a hypothetical protein similar to PA-IIL and coded by the gene cv1741 was found. The gene was cloned and

Název v anglickém jazyce

Sructure-function characterisation of a new lectin from Chromobacterium violaceum

Popis výsledku anglicky

Carbohydrates are essential components of life that play crucial role in all organisms. They are very important agent in recognition and signalling ways. Lectin-carbohydrate interactions play a crucial role in many recognition events. Pseudomonas aeruginosa, an opportunistic pathogen responsible for numerous nosocomial infections in immunocopromised patients, produces a variety of carbohydrate-binding proteins that could be involved in host recognition and adhesion. One of them, PA-IIL, is a fucose binding lectin that is closely related to the virulence of the bacterium [1]. Searching in databases for proteins displaying sequence similarities to PA-IIL revealed new homologous proteins in other opportunistic pathogens like Chromobacterium violaceum. Human infection by Ch. violaceum is rare but when it occurs, it is associated with very high mortality rate [2]. In Ch. violaceum genome a hypothetical protein similar to PA-IIL and coded by the gene cv1741 was found. The gene was cloned and

Druh

D - Stať ve sborníku

CEP obor

CE - Biochemie

OECD FORD obor

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Projekt

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Návaznosti

Z - Vyzkumny zamer (s odkazem do CEZ)

Rok uplatnění

2005

Kód důvěrnosti údajů

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

Název statě ve sborníku

The FEBS Journal

ISBN

1474-3833

ISSN

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e-ISSN

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Počet stran výsledku

1

Strana od-do

16

Název nakladatele

FEBS Congres

Místo vydání

Budapest

Místo konání akce

Budapest

Datum konání akce

2. 7. 2005

Typ akce podle státní příslušnosti

WRD - Celosvětová akce

Kód UT WoS článku

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