Taxonomic group: bacteria / Proteobacteria
(Phylum: Proteobacteria)
Host organism: Homo sapiens
Associated disease: bacteremia [ICD11:
MA15.0 
];
septicemia [ICD11:
MA15.Y ]
The structure was elucidated in this paperNCBI PubMed ID: 21890891Publication DOI: 10.1093/glycob/cwr119Journal NLM ID: 9104124Publisher: IRL Press at Oxford University Press
Correspondence: czaja
iitd.pan.wroc.pl
Institutions: Laboratory of Immunobiology of Infections, Institute for Medical Biology, Polish Academy of Sciences, Lodowa 106, PL-93-232 Lodz, Poland
The ficolin-1 (M), -2 (L), -3 (H) and mannan-binding lectin (MBL) activate the complement system and have opsonic activity. The specificity of ficolin-3 is poorly characterised and currently limited to a few ligands only. We present new specific targets for human ficolin-3, identified among lipopolysaccharides (LPS, endotoxin) of Hafnia alvei. The interaction was restricted to LPSs of four strains: 23, PCM 1200, PCM 1203, PCM 1205 and limited to their O-specific polysaccharides (O-specific PS) composed of different number of oligosaccharide repeating units (RU). Moreover, these LPS/Ficolin-3 complexes activated the lectin pathway of complement in a C4b-deposition assay in calcium- and magnesium-dependent way.A neoglycoconjugate of the O-specific PS fraction of H. alvei 1200 LPS with BSA was prepared and used as a tool for determination of ficolin-3 concentration and activity in serum. To confirm a structure of the O-specific PS 1200 selected for the conjugate preparation, structural analysis was performed on a series of O-specific PSs released by mild acid hydrolysis of the LPS. The isolated O-specific PSs, showed the different length distribution, were devoid of a major part of core oligosaccharide region and had Hep-Kdo disaccharide at a reducing end. The neoglycoconjugate was a highly selective tool for determination of ficolin-3 concentration and activity in serum (lectin pathway activation in C4b deposition assay) and was not affected by MBL, ficolin-1 and ficolin-2 or natural antibodies.
Lipopolysaccharide, endotoxin, Hafnia, complement, ficolin
Structure type: polymer chemical repeating unit ; n=1-3
Location inside paper: p.271, fig.4A, p.273, fig.5
Compound class: O-polysaccharide
Contained glycoepitopes: IEDB_135813,IEDB_136044,IEDB_137340,IEDB_137472,IEDB_141794,IEDB_141807,IEDB_142078,IEDB_142488,IEDB_144998,IEDB_146664,IEDB_150899,IEDB_151531,IEDB_190606,IEDB_983931,SB_137,SB_165,SB_166,SB_187,SB_192,SB_195,SB_29,SB_7,SB_88
Methods: 13C NMR, 1H NMR, NMR-2D, SDS-PAGE, sugar analysis, mild acid hydrolysis, Western blotting, MALDI-TOF MS, serological methods, conjugation
Biological activity: interaction of ficolin-3 with H. alvei LPSs
Comments, role: Part of the O-polysaccharide (see RR: 28659); PS1-PS3: n=1-2,PS4: n=2,PS5: n=1; αDGlcp residue is missing in the first RU for PS1-PS5.
Related record ID(s): 28659, 28867
NCBI Taxonomy refs (TaxIDs): 569Reference(s) to other database(s): GTC:G72612BZ
Show glycosyltransferases
There is only one chemically distinct structure:
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