The fucose-binding lectin from Ralstonia solanacearum: a new
type of beta-propeller architecture formed by oligomerisation
and interacting with fucoside, fucosyllactose and plant
xyloglucan

J 2005

The fucose-binding lectin from Ralstonia solanacearum: a new type of beta-propeller architecture formed by oligomerisation and interacting with fucoside, fucosyllactose and plant xyloglucan

KOSTLÁNOVÁ, Nikola, Edward MITCHELL, Hugues LORTAT-JACOB, Stefan OSCARSON, Martina LAHMANN et. al.

Základní údaje

Originální název

The fucose-binding lectin from Ralstonia solanacearum: a new type of beta-propeller architecture formed by oligomerisation and interacting with fucoside, fucosyllactose and plant xyloglucan

Název česky

Fukosu vazajici lektin z Ralstonia solanacearum: novy typ beta barelu tvoreny oligomerizaci a interakce s fukosidem, fukosyllaktosou a rostlinnym xyloglukanem

Autoři

KOSTLÁNOVÁ, Nikola (203 Česká republika), Edward MITCHELL (826 Velká Británie a Severní Irsko), Hugues LORTAT-JACOB (250 Francie), Stefan OSCARSON (752 Švédsko), Martina LAHMANN (752 Švédsko), Nechama GILBOA-GARBER (376 Izrael), Gerard CHAMBAT (250 Francie), Michaela WIMMEROVÁ (203 Česká republika, garant) a Anne IMBERTY (250 Francie)

Vydání

Journal of Biological Chemistry, Bethesda, USA, Amer. Soc. Biochem. Mol. Biol. 2005, 0021-9258

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

10600 1.6 Biological sciences

Stát vydavatele

Spojené státy

Utajení

není předmětem státního či obchodního tajemství

Impakt faktor

Impact factor: 5.854

Kód RIV

RIV/00216224:14310/05:00013768

Organizační jednotka

Přírodovědecká fakulta

UT WoS

000230678600045

Klíčová slova anglicky

lectin; Ralstonia solanacearum; crystal structure; propeller; SPR

Štítky

Crystal Structure, lectin, propeller, ralstonia solanacearum, SPR

Příznaky

Mezinárodní význam, Recenzováno

Změněno: 4. 1. 2007 15:32, prof. RNDr. Michaela Wimmerová, Ph.D.

Anotace

ORIG CZ

V originále

Plant pathogens, as animal ones, use protein-carbohydrate interactions in their strategy for host recognition, attachment and invasion. The bacterium Ralstonia solanacearum which is distributed worldwide and causes lethal wilt in many agricultural crops, was shown to produce a potent L-fucose-binding lectin, RSL, a small protein of 90 amino acids with a tandem repeat in its amino acid sequence. In the present study, surface plasmon resonance experiments conducted on a series of oligosaccharides show a preference for binding to áFuc1-2Gal and áFuc1-6Gal epitopes. Titration microcalorimetry demonstrates the presence of two binding sites per monomer and an unusually high affinity of the lectin for áFuc1-2Gal containing oligosaccharides (KD 2.5 10-7 M for 2-fucosyllactose). RSL has been crystallised with a methyl derivative of fucose and with the highest affinity ligand, 2-fucosyllactose. X-ray crystal structures, the one with á-methyl-fucoside being at ultra-high resolution, reveal that each monomer consists of two small fourstranded anti-parallel â-sheets. Trimerisation through 3-fold or pseudo 3- fold axis generates a six-bladed â-propeller architecture, very similar to that previously described for the fungal lectin of Aleuria aurantia. This is the first report of a â- propeller formed by oligomerisation and not by sequential domains. Each monomer presents two fucose binding sites, resulting in six symmetrically arranged sugar binding sites for the â-propeller. Crystals were also obtained for a mutated lectin complexed with a fragment of xyloglucan, a fucosylated polysaccharides from the primary cell wall of plants, which may be the biological target of the lectin.

Česky

Fukosu vazajici lektin z Ralstonia solanacearum: novy typ beta barelu tvoreny oligomerizaci a interakce s fukosidem, fukosyllaktosou a rostlinnym xyloglukanem

Návaznosti

LN00A016, projekt VaV

Název: BIOMOLEKULÁRNÍ CENTRUM

Investor: Ministerstvo školství, mládeže a tělovýchovy ČR, Biomolekulární centrum

MSM0021622413, záměr

Název: Proteiny v metabolismu a při interakci organismů s prostředím

Investor: Ministerstvo školství, mládeže a tělovýchovy ČR, Proteiny v metabolismu a při interakci organismů s prostředím

Citovat

KOSTLÁNOVÁ, Nikola, Edward MITCHELL, Hugues LORTAT-JACOB, Stefan OSCARSON, Martina LAHMANN, Nechama GILBOA-GARBER, Gerard CHAMBAT, Michaela WIMMEROVÁ a Anne IMBERTY. The fucose-binding lectin from Ralstonia solanacearum: a new type of beta-propeller architecture formed by oligomerisation and interacting with fucoside, fucosyllactose and plant xyloglucan. Journal of Biological Chemistry. Bethesda, USA: Amer. Soc. Biochem. Mol. Biol., 2005, roč. 280, č. 30, s. 27839-27849. ISSN 0021-9258.

@article{571969,
   author = {Kostlánová, Nikola and Mitchell, Edward and LortatandJacob, Hugues and Oscarson, Stefan and Lahmann, Martina and GilboaandGarber, Nechama and Chambat, Gerard and Wimmerová, Michaela and Imberty, Anne},
   article_location = {Bethesda, USA},
   article_number = {30},
   keywords = {lectin; Ralstonia solanacearum; crystal structure; propeller; SPR},
   language = {eng},
   issn = {0021-9258},
   journal = {Journal of Biological Chemistry},
   title = {The fucose-binding lectin from Ralstonia solanacearum: a new type of beta-propeller architecture formed by oligomerisation and interacting with fucoside, fucosyllactose and plant xyloglucan},
   volume = {280},
   year = {2005}
}

TY  - JOUR
ID  - 571969
AU  - Kostlánová, Nikola - Mitchell, Edward - Lortat-Jacob, Hugues - Oscarson, Stefan - Lahmann, Martina - Gilboa-Garber, Nechama - Chambat, Gerard - Wimmerová, Michaela - Imberty, Anne
PY  - 2005
TI  - The fucose-binding lectin from Ralstonia solanacearum: a new type of beta-propeller architecture formed by oligomerisation and interacting with fucoside, fucosyllactose and plant xyloglucan
JF  - Journal of Biological Chemistry
VL  - 280
IS  - 30
SP  - 27839-27849
EP  - 27839-27849
PB  - Amer. Soc. Biochem. Mol. Biol.
SN  - 00219258
KW  - lectin
KW  - Ralstonia solanacearum
KW  - crystal structure
KW  - propeller
KW  - SPR
N2  - Plant pathogens, as animal ones, use protein-carbohydrate interactions in their strategy for host recognition, attachment and invasion. The bacterium Ralstonia solanacearum which is distributed worldwide and causes lethal wilt in many agricultural crops, was shown to produce a potent L-fucose-binding lectin, RSL, a small protein of 90 amino acids with a tandem repeat in its amino acid sequence. In the present study, surface plasmon resonance experiments conducted on a series of oligosaccharides show a preference for binding to áFuc1-2Gal and áFuc1-6Gal epitopes. Titration microcalorimetry demonstrates the presence of two binding sites per monomer and an unusually high affinity of the lectin for áFuc1-2Gal containing oligosaccharides (KD 2.5 10-7 M for 2-fucosyllactose). RSL has been crystallised with a methyl derivative of fucose and with the highest affinity ligand, 2-fucosyllactose. X-ray crystal structures, the one with á-methyl-fucoside being at ultra-high resolution, reveal that each monomer consists of two small fourstranded anti-parallel â-sheets. Trimerisation through 3-fold or pseudo 3- fold axis generates a six-bladed â-propeller architecture, very similar to that previously described for the fungal lectin of Aleuria aurantia. This is the first report of a â- propeller formed by oligomerisation and not by sequential domains. Each monomer presents two fucose binding sites, resulting in six symmetrically arranged sugar binding sites for the â-propeller. Crystals were also obtained for a mutated lectin complexed with a fragment of xyloglucan, a fucosylated polysaccharides from the primary cell wall of plants, which may be the biological target of the lectin.
ER  -

KOSTLÁNOVÁ, Nikola, Edward MITCHELL, Hugues LORTAT-JACOB, Stefan OSCARSON, Martina LAHMANN, Nechama GILBOA-GARBER, Gerard CHAMBAT, Michaela WIMMEROVÁ a Anne IMBERTY. The fucose-binding lectin from Ralstonia solanacearum: a new type of beta-propeller architecture formed by oligomerisation and interacting with fucoside, fucosyllactose and plant xyloglucan. \textit{Journal of Biological Chemistry}. Bethesda, USA: Amer. Soc. Biochem. Mol. Biol., 2005, roč.~280, č.~30, s.~27839-27849. ISSN~0021-9258.

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