Specificity and kinetics of oligosaccharide recognition by RSL, a fucose-binding lectin from the plant pathogen Ralstonia solanacearum.

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14310%2F03%3A00008866" target="_blank" >RIV/00216224:14310/03:00008866 - isvavai.cz</a>

Výsledek na webu

—

DOI - Digital Object Identifier

—

Jazyk výsledku

angličtina

Název v původním jazyce

Specificity and kinetics of oligosaccharide recognition by RSL, a fucose-binding lectin from the plant pathogen Ralstonia solanacearum.

Popis výsledku v původním jazyce

Ralstonia solanacearum is a worldwide distributed plant aggressive pathogen which causes lethal wilt in many crops. Its extracts contain a fucose-binding lectin that has been recently purified and characterized [1]. Its 90 amino acid sequence contains two repeating domains, with strong similarity to the fucose-binding lectin of the mushroom Aleuria aurantia (AAL), which is also a soil inhabitant. Surface plasmon resonance experiments demonstrate that the lectin binds strongly to fragments of fucose-containing xyloglucan polysaccharide purified from plant cell walls. This binding can diversely be inhibited by fucose and fucose-containing oligosaccharides. Best inhibition was obtained with oligosaccharides containing an aFuc(1-2)Gal terminal disaccharide, particularly XG9 (Glc4 Xyl3 Gal Fuc) which is a structurally well determined plant oligosaccharide that has previously been demonstrated to have biological activity in plants [2]. Our results are in agreement with the assumption that RS

Název v anglickém jazyce

Specificity and kinetics of oligosaccharide recognition by RSL, a fucose-binding lectin from the plant pathogen Ralstonia solanacearum.

Popis výsledku anglicky

Ralstonia solanacearum is a worldwide distributed plant aggressive pathogen which causes lethal wilt in many crops. Its extracts contain a fucose-binding lectin that has been recently purified and characterized [1]. Its 90 amino acid sequence contains two repeating domains, with strong similarity to the fucose-binding lectin of the mushroom Aleuria aurantia (AAL), which is also a soil inhabitant. Surface plasmon resonance experiments demonstrate that the lectin binds strongly to fragments of fucose-containing xyloglucan polysaccharide purified from plant cell walls. This binding can diversely be inhibited by fucose and fucose-containing oligosaccharides. Best inhibition was obtained with oligosaccharides containing an aFuc(1-2)Gal terminal disaccharide, particularly XG9 (Glc4 Xyl3 Gal Fuc) which is a structurally well determined plant oligosaccharide that has previously been demonstrated to have biological activity in plants [2]. Our results are in agreement with the assumption that RS

Druh

D - Stať ve sborníku

CEP obor

CE - Biochemie

OECD FORD obor

—

Projekt

<a href="/cs/project/LN00A016" target="_blank" >LN00A016: BIOMOLEKULÁRNÍ CENTRUM</a><br>

Návaznosti

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

Rok uplatnění

2003

Kód důvěrnosti údajů

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

Název statě ve sborníku

XVII International Symposium on Glycoconjugates

ISBN

—

ISSN

—

e-ISSN

—

Počet stran výsledku

1

Strana od-do

23

Název nakladatele

AS

Místo vydání

Bangalore, Indie

Místo konání akce

Bangalore, Indie

Datum konání akce

1. 1. 2003

Typ akce podle státní příslušnosti

WRD - Celosvětová akce

Kód UT WoS článku

—