Sructure-function characterisation of a new lectin from Chromobacterium violaceum
The result's identifiers
Result code in 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>
Result on the web
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DOI - Digital Object Identifier
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Alternative languages
Result language
angličtina
Original language name
Sructure-function characterisation of a new lectin from Chromobacterium violaceum
Original language description
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
Czech name
Strukturně funkční charakterizace nového lektinu z bakterie Chromobacterium violaceum
Czech description
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
Classification
Type
D - Article in proceedings
CEP classification
CE - Biochemistry
OECD FORD branch
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Result continuities
Project
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Continuities
Z - Vyzkumny zamer (s odkazem do CEZ)
Others
Publication year
2005
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Article name in the collection
The FEBS Journal
ISBN
1474-3833
ISSN
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e-ISSN
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Number of pages
1
Pages from-to
16
Publisher name
FEBS Congres
Place of publication
Budapest
Event location
Budapest
Event date
Jul 2, 2005
Type of event by nationality
WRD - Celosvětová akce
UT code for WoS article
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