Taxonomic group: bacteria / Proteobacteria
(Phylum: Proteobacteria)
Host organism: Bos taurus
Associated disease: infectious bovine keratoconjunctivitis [ICD11:
9A60.3Z 
, ICD11:
9A60.Y ];
infection due to Moraxella [ICD11:
XN90V ]
The structure was elucidated in this paperNCBI PubMed ID: 26774874Publication DOI: 10.1016/j.carres.2015.12.003Journal NLM ID: 0043535Publisher: Elsevier
Correspondence: jennifer.wilson
griffith.edu.au; i.peak
griffith.edu.au
Institutions: Menzies Health Institute, Molecular Basis of Disease, Griffith University, Gold Coast Campus, Southport, Qld. 4222, Australia, Institute for Glycomics, Griffith University, Gold Coast Campus, Southport, Qld. 4222, Australia, School of Medical Science, Griffith University, Gold Coast Campus, Southport, Qld. 4222, Australia
Moraxella bovis is a Gram-negative gammaproteobacterium and is one of the causative agents of infectious bovine keratoconjunctivitis. The structure of lipooligosaccharide (LOS) from strain Epp63 was recently elucidated. In the present study a genetic locus of seven encoding genes with high similarity to glycosyltransferases has been identified. Mutation of these putative glycosyltransferase genes resulted in M. bovis mutant bacteria that expressed truncated LOS structures. The structures of the oligosaccharide (OS) expressed by the mutant strains were elucidated and demonstrated the role of the glycosyltransferase enzymes in the LOS biosynthesis of M. bovis. The glycosyltransferase genes designated lgt1, lgt3, and lgt6 are highly similar to the genes in the related bacterium M. catarrhalis. In addition, there are syntenic similarities with the corresponding LOS biosynthesis locus in M. catarrhalis and other members of Moraxellaceae.
Lipooligosaccharide, glycosyltransferase, lipo-oligosaccharide, Infectious bovine keratoconjunctivitis, Moraxella bovis
Structure type: oligomer
Location inside paper: p.12, fig.3, 63.1∆
Compound class: LOS
Contained glycoepitopes: IEDB_130650,IEDB_141806,IEDB_142488,IEDB_144998,IEDB_146664,IEDB_983931,SB_192
Methods: 13C NMR, 1H NMR, NMR-2D, PCR, SDS-PAGE, sugar analysis, acid hydrolysis, NMR-1D, genetic methods, GPC, bioinformatic analysis, SEC
Biological activity: the role of the glycosyltransferase enzymes in the LOS biosynthesis of M. bovis
Related record ID(s): 11254, 11598, 11599
NCBI Taxonomy refs (TaxIDs): 476Reference(s) to other database(s): GTC:G74587GM
Show glycosyltransferases
NMR conditions: in D2O at 298 K
[as TSV]
13C NMR data:
Linkage Residue C1 C2 C3 C4 C5 C6 C7 C8
5,4 bDGlcp 103.2 74.1 76.6 70.5 76.8 61.7
5,6 bDGlcp 103.2 74.1 76.8 70.6 76.8 61.7
5 aDGlcp 100.4 72.7 72.6 78.8 70.4 68.0
aXKdo? ? ? 40.2 67.1 76.5 72.6 68.5 63.5
1H NMR data:
Linkage Residue H1 H2 H3 H4 H5 H6 H7 H8
5,4 bDGlcp 4.58 3.26 3.50 3.39 3.45 3.74-3.93
5,6 bDGlcp 4.49 3.23 3.49 3.39 3.44 3.72-3.92
5 aDGlcp 5.13 3.58 3.89 3.77 4.36 3.98-4.13
aXKdo? - - 1.81-2.19 4.13 4.06 3.81 4.01 3.59-3.82
1H/13C HSQC data:
Linkage Residue C1/H1 C2/H2 C3/H3 C4/H4 C5/H5 C6/H6 C7/H7 C8/H8
5,4 bDGlcp 103.2/4.58 74.1/3.26 76.6/3.50 70.5/3.39 76.8/3.45 61.7/3.74-3.93
5,6 bDGlcp 103.2/4.49 74.1/3.23 76.8/3.49 70.6/3.39 76.8/3.44 61.7/3.72-3.92
5 aDGlcp 100.4/5.13 72.7/3.58 72.6/3.89 78.8/3.77 70.4/4.36 68.0/3.98-4.13
aXKdo? 40.2/1.81-2.19 67.1/4.13 76.5/4.06 72.6/3.81 68.5/4.01 63.5/3.59-3.82
1H NMR data:
| Linkage | Residue | H1 | H2 | H3 | H4 | H5 | H6 | H7 | H8 |
|---|
| 5,4 | bDGlcp | 4.58 | 3.26 | 3.50 | 3.39 | 3.45 | 3.74
3.93 | |
| 5,6 | bDGlcp | 4.49 | 3.23 | 3.49 | 3.39 | 3.44 | 3.72
3.92 | |
| 5 | aDGlcp | 5.13 | 3.58 | 3.89 | 3.77 | 4.36 | 3.98
4.13 | |
| | aXKdo? |
|
| 1.81
2.19 | 4.13 | 4.06 | 3.81 | 4.01 | 3.59
3.82 |
|
13C NMR data:
| Linkage | Residue | C1 | C2 | C3 | C4 | C5 | C6 | C7 | C8 |
|---|
| 5,4 | bDGlcp | 103.2 | 74.1 | 76.6 | 70.5 | 76.8 | 61.7 | |
| 5,6 | bDGlcp | 103.2 | 74.1 | 76.8 | 70.6 | 76.8 | 61.7 | |
| 5 | aDGlcp | 100.4 | 72.7 | 72.6 | 78.8 | 70.4 | 68.0 | |
| | aXKdo? | ? | ? | 40.2 | 67.1 | 76.5 | 72.6 | 68.5 | 63.5 |
|
![](nmr_drawer.py?width=750&height=130&nucleus=C&rotate_labels=false&spectrum=[{"s":103.2,"l":"1","c":[0,0,225]},{"s":74.1,"l":"2","c":[0,0,225]},{"s":76.6,"l":"3","c":[0,0,225]},{"s":70.5,"l":"4","c":[0,0,225]},{"s":76.8,"l":"5","c":[0,0,225]},{"s":61.7,"l":"6","c":[0,0,225]},{"s":103.2,"l":"1","c":[230,0,30]},{"s":74.1,"l":"2","c":[230,0,30]},{"s":76.8,"l":"3","c":[230,0,30]},{"s":70.6,"l":"4","c":[230,0,30]},{"s":76.8,"l":"5","c":[230,0,30]},{"s":61.7,"l":"6","c":[230,0,30]},{"s":100.4,"l":"1","c":[0,165,0]},{"s":72.7,"l":"2","c":[0,165,0]},{"s":72.6,"l":"3","c":[0,165,0]},{"s":78.8,"l":"4","c":[0,165,0]},{"s":70.4,"l":"5","c":[0,165,0]},{"s":68,"l":"6","c":[0,165,0]},{"s":40.2,"l":"3","c":[120,0,225]},{"s":67.1,"l":"4","c":[120,0,225]},{"s":76.5,"l":"5","c":[120,0,225]},{"s":72.6,"l":"6","c":[120,0,225]},{"s":68.5,"l":"7","c":[120,0,225]},{"s":63.5,"l":"8","c":[120,0,225]}])
The spectrum also has 2 signals at unknown positions (not plotted). |
There is only one chemically distinct structure:
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