One point mutation can overturn sugar-binding specificity of lectin RS-IIL from plant pathogen Ralstonia solanacearum

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14310%2F15%3A00087734" target="_blank" >RIV/00216224:14310/15:00087734 - 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

One point mutation can overturn sugar-binding specificity of lectin RS-IIL from plant pathogen Ralstonia solanacearum

Popis výsledku v původním jazyce

A soil bacterium Ralstonia solanacearum is an aggressive phytopathogen which causes severe wilts of many economically important crops in tropical and subtropical regions. This pathogen produces two lectins: RSL and RS-IIL. Lectins are sugar-binding proteins different from sugar-specific antibodies or enzymes. They often play an important role in host-pathogen recognition and interactions. Lectin RS-IIL belongs to a so-called “PA-IIL family”, which includes also lectins PA-IIL (from P. aeruginosa), CV-IIL (from C. violaceum), BC2L-A and BC2L-C (from B. cenocepacia). These lectins are orthologs with significant sequential and structural similarities. Although they bind saccharides with similar stereochemistry, they differ in preferences towards these saccharides. This fact is caused by differences in three amino acids which are arranged in the so-called “specificity binding loop”. Adam et al. prepared three point mutants of the PA-IIL lectin to investigate the fine specificity.

Název v anglickém jazyce

One point mutation can overturn sugar-binding specificity of lectin RS-IIL from plant pathogen Ralstonia solanacearum

Popis výsledku anglicky

A soil bacterium Ralstonia solanacearum is an aggressive phytopathogen which causes severe wilts of many economically important crops in tropical and subtropical regions. This pathogen produces two lectins: RSL and RS-IIL. Lectins are sugar-binding proteins different from sugar-specific antibodies or enzymes. They often play an important role in host-pathogen recognition and interactions. Lectin RS-IIL belongs to a so-called “PA-IIL family”, which includes also lectins PA-IIL (from P. aeruginosa), CV-IIL (from C. violaceum), BC2L-A and BC2L-C (from B. cenocepacia). These lectins are orthologs with significant sequential and structural similarities. Although they bind saccharides with similar stereochemistry, they differ in preferences towards these saccharides. This fact is caused by differences in three amino acids which are arranged in the so-called “specificity binding loop”. Adam et al. prepared three point mutants of the PA-IIL lectin to investigate the fine specificity.

Druh

O - Ostatní výsledky

CEP obor

CE - Biochemie

OECD FORD obor

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Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Rok uplatnění

2015

Kód důvěrnosti údajů

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