J 2010

A TNF-like Trimeric Lectin Domain from Burkholderia cenocepacia with Specificity for Fucosylated Human Histo-Blood Group Antigens

ŠULÁK, Ondřej, Gianluca CIOCI, Monia DELIA, Martina LAHMANN, Annabelle VARROT et. al.

Basic information

Original name

A TNF-like Trimeric Lectin Domain from Burkholderia cenocepacia with Specificity for Fucosylated Human Histo-Blood Group Antigens

Name in Czech

A TNF-like Trimeric Lectin Domain from Burkholderia cenocepacia with Specificity for Fucosylated Human Histo-Blood Group Antigens

Authors

ŠULÁK, Ondřej (203 Czech Republic, belonging to the institution), Gianluca CIOCI (250 France), Monia DELIA (380 Italy, belonging to the institution), Martina LAHMANN (826 United Kingdom of Great Britain and Northern Ireland), Annabelle VARROT (250 France), Anne IMBERTY (250 France) and Michaela WIMMEROVÁ (203 Czech Republic, guarantor, belonging to the institution)

Edition

Structure, CAMBRIDGE, CELL PRESS, 2010, 0969-2126

Other information

Language

English

Type of outcome

Článek v odborném periodiku

Field of Study

10404 Polymer science

Country of publisher

United States of America

Confidentiality degree

není předmětem státního či obchodního tajemství

References:

Impact factor

Impact factor: 6.337

RIV identification code

RIV/00216224:14310/10:00057175

Organization unit

Faculty of Science

DOI

UT WoS

000273859700010

Keywords (in Czech)

lektin; Burkholderia cenocepacia; patogen; TNF

Keywords in English

lectin; Burkholderia cenocepacia; pathogen; TNF

Tags

Tags

International impact, Reviewed
Změněno: 31/10/2012 10:38, Olga Křížová

Abstract

ORIG CZ

V originále

The opportunistic pathogen Burkholderia cenocepacia expresses several soluble lectins, among them BC2L-C. This lectin exhibits two domains: a C-terminal domain with high sequence similarity to the recently described calcium-dependent mannose-binding lectin BC2L-A, and an N-terminal domain of 156 amino acids without similarity to any known protein. The recombinant N-terminal BC2L-C domain is a new lectin with specificity for fucosylated human histo-blood group epitopes H-type 1, Lewis b, and Lewis Y, as determined by glycan array and isothermal titration calorimetry. Methylselenofucoside was used as ligand to solve the crystal structure of the N-terminal BC2L-C domain. Additional molecular modeling studies rationalized the preference for Lewis epitopes. The structure reveals a trimeric jellyroll arrangement with striking similarity to TNF-like proteins, and to BclA, the spore protein from Bacillus anthracis which may play an important role in bioadhesion of anthrax spores in human lungs.

In Czech

Podmíněný patogen Burkholderia cenocepacia produkuje několik rozpustných lektinů. Trimerní N-terminální doména BC2L-C-nt podobná TNF z podmíněného patogenu Burkholderia cenocepacia vykazuje specifitu vůči fukosylovaným lidským krevním antigenům.

Links

GA303/09/1168, research and development project
Name: Lektiny z lidských patogenů - struktura, funkce, inženýrství
Investor: Czech Science Foundation, Lectins from human pathogens - structure, function, engineering
GD301/09/H004, research and development project
Name: Molekulární a strukturní biologie vybraných cytostatik. Od mechanistických studií k chemoterapii rakoviny
Investor: Czech Science Foundation
LC06030, research and development project
Name: Biomolekulární centrum
Investor: Ministry of Education, Youth and Sports of the CR, Biomolecular centre
MSM0021622413, plan (intention)
Name: Proteiny v metabolismu a při interakci organismů s prostředím
Investor: Ministry of Education, Youth and Sports of the CR, Proteins in metabolism and interaction of organisms with the environment
205872, interní kód MU
Name: Program developing interdisciplinary research POtential for the STudies of BIOMolecular INteractions (Acronym: POSTBIOMIN)
Investor: European Union, Program developing interdisciplinary research POtential for the STudies of BIOMolecular INteractions, Capacities