Pa-IIl-Like Lectins In Human Pathogen Burkholderia Cenocepacia

Investor logo
Investor logo

Warning

This publication doesn't include Faculty of Economics and Administration. It includes Faculty of Science. Official publication website can be found on muni.cz.
Title in English Pa-Iil-Like Lectins In Human Pathogen Burkholderia Cenocepacia
Authors

ŠULÁK Ondřej MALINOVSKÁ Lenka LAMEIGNERE Emilie VARROT Annabelle IMBERTY Anne WIMMEROVÁ Michaela

Year of publication 2009
Type Article in Proceedings
Conference 15th Europian Carbohydrate Symposium
MU Faculty or unit

Faculty of Science

Citation
Field Biochemistry
Keywords Burkholderia cenocepacia; lectin; structure function characterisation;
Description Pathogen recognition and adhesion to the host cell surface is usually mediated by protein-carbohydrate interactions. Chronic pulmonary colonization by opportunistic pathogens like Pseudomonas aeruginosa or bacteria associated with so-called Burkholderia cepacia complex (BCC) is the main reason of death among cystic fibrosis patients. Searching in databases for proteins displaying sequence similarities to PAIIL revealed new homologous proteins in other opportunistic pathogens like Chromobacterium violaceum, Ralstonia solanacearum and even three to four copies, depending on the strain, in Burkholderia cenocepacia, a member of BCC. The contribution is focused on structure-function characterisation of lectins from B. cenocepacia that we identified in its genome. All of the can bind to fucosylated and/or mannosylated oligosaccharides. Except the shortest one, BclA, other three proteins contain an extended N terminal domain of unknown function showing no sequence similarity with any protein in amino acid databases.
Related projects:

You are running an old browser version. We recommend updating your browser to its latest version.