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Characterization of novel lectins from Burkholderia pseudomallei and Chromobacterium violaceum with seven-bladed β-propeller fold
P. Sýkorová, J. Novotná, G. Demo, G. Pompidor, E. Dubská, J. Komárek, E. Fujdiarová, J. Houser, L. Hároníková, A. Varrot, N. Shilova, A. Imberty, N. Bovin, M. Pokorná, M. Wimmerová
Jazyk angličtina Země Nizozemsko
Typ dokumentu časopisecké články
- MeSH
- bakteriální proteiny metabolismus MeSH
- Burkholderia pseudomallei metabolismus MeSH
- Chromobacterium metabolismus MeSH
- fukosa metabolismus MeSH
- lektiny metabolismus MeSH
- lidé MeSH
- monosacharidy metabolismus MeSH
- polysacharidy metabolismus MeSH
- zvířata MeSH
- Check Tag
- lidé MeSH
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
Burkholderia pseudomallei and Chromobacterium violaceum are bacteria of tropical and subtropical soil and water that occasionally cause fatal infections in humans and animals. Microbial lectins mediate the adhesion of organisms to host cells, which is the first phase in the development of infection. Here we report the discovery of two novel lectins from the above-mentioned bacteria - BP39L and CV39L. The crystal structures revealed that the lectins possess a seven-bladed β-propeller fold. Functional studies conducted on a series of oligo- and polysaccharides confirmed the preference of BP39L for mannosylated saccharides and CV39L for rather more complex polysaccharides with a monosaccharide preference for β-l-fucose. The presented data indicate that the proteins belong to a currently unknown family of lectins.
Central European Institute of Technology Masaryk University Brno Czech Republic
CERMAV CNRS Université de Grenoble Alpes Grenoble France
Department of Biochemistry Faculty of Science Masaryk University Brno Czech Republic
EMBL Hamburg c o DESY Hamburg Germany
National Centre for Biomolecular Research Faculty of Science Masaryk University Brno Czech Republic
Citace poskytuje Crossref.org
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- $a Burkholderia pseudomallei and Chromobacterium violaceum are bacteria of tropical and subtropical soil and water that occasionally cause fatal infections in humans and animals. Microbial lectins mediate the adhesion of organisms to host cells, which is the first phase in the development of infection. Here we report the discovery of two novel lectins from the above-mentioned bacteria - BP39L and CV39L. The crystal structures revealed that the lectins possess a seven-bladed β-propeller fold. Functional studies conducted on a series of oligo- and polysaccharides confirmed the preference of BP39L for mannosylated saccharides and CV39L for rather more complex polysaccharides with a monosaccharide preference for β-l-fucose. The presented data indicate that the proteins belong to a currently unknown family of lectins.
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