Jimenez N, Lacasta A, Vilches S, Reyes M, Vazquez J, Aquillini E, Merino S, Regue M, Tomas JM Genetics and proteomics of Aeromonas salmonicida lipopolysaccharide core biosynthesis Journal of Bacteriology191(7) (2009)
2228-2236
a-D-GlcpN-(1-7)-L-gro-a-D-manHepp-(1-2)-L-gro-a-D-manHepp-(1-3)-+ P-4)-+
| |
/Variants 0/-L-gro-a-D-manHepp-(1-6)-b-D-Glcp-(1-4)-L-gro-a-D-manHepp-(1-5)-a-Kdop-(2--/lipid A/
|
L-gro-a-D-manHepp-(1-6)-+
/Variants 0/ is:
a-D-Galp-(1-4)-b-D-GalpNAc-(1-4)-
OR (exclusively)
a-D-Galp-(1-4)-
NCBI PubMed ID:19151135 Publication DOI:10.1128/JB.01395-08 Journal NLM ID:2985120R Publisher: American Society for Microbiology Correspondence: jtomasub.edu Institutions: Departamento de Microbiologia, Facultad de Biologia, Universidad de Barcelona, Diagonal 645, 08071 Barcelona, Spain, Departamento de Microbiologia y Parasitologia Sanitarias, Facultad de Farmacia, Universidad de Barcelona, Av. Joan XXIII s/n, 08028 Barcelona, Spain
Comparison between the lipopolysaccharide (LPS) core structures of Aeromonas salmonicida subsp. salmonicida A450 and Aeromonas hydrophila AH-3 shows great similarity in the inner LPS core and part of the outer LPS core but some differences in the distal part of the outer LPS core (residues ld-Hep, d-Gal, and d-GalNAc). The three genomic regions encoding LPS core biosynthetic genes in A. salmonicida A450, of which regions 2 and 3 have genes identical to those of A. hydrophila AH-3, were fully sequenced. A. salmonicida A450 region 1 showed seven genes: three identical to those of A. hydrophila AH-3, three similar but not identical to those of A. hydrophila AH-3, and one without any homology to any well-characterized gene. A. salmonicida A450 mutants with alterations in the genes that were not identical to those of A. hydrophila AH-3 were constructed, and their LPS core structures were fully elucidated. At the same time, all the A. salmonicida A450 genes identical to those of A. hydrophila AH-3 were used to complement the previously obtained A. hydrophila AH-3 mutants for each of these genes. Combining the gene sequence and complementation test data with the structural data and phenotypic characterization of the mutant LPSs enabled a presumptive assignment of all LPS core biosynthesis gene functions in A. salmonicida A450. Furthermore, hybridization studies with internal probes for the A. salmonicida-specific genes using different A. salmonicida strains (strains of different subspecies or atypical strains) showed a unique or prevalent LPS core type, which is the one fully characterized for A. salmonicida A450.
Jimenez N, Vilches S, Lacasta A, Regue M, Merino S, Tomas JM A bifunctional enzyme in a single gene catalyzes the incorporation of GlcN into the Aeromonas core LPS Journal of Biological Chemistry284(48) (2009)
32995-33005
NCBI PubMed ID:19805547 Journal NLM ID:2985121R Publisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology Correspondence: jtomasub.edu Institutions: Department Microbiologia University Barcelona, Spain
The core lipopolysaccharide (LPS) of Aeromonas hydrophila AH-3 and A. salmonicida A450 is characterized by the presence of the pentasaccharide α-D-GlcN-(1-7)-L-α-D-Hep-(1-2)-L-α-D-Hep-(1-3)-L-α-D-Hep-(1-5)-α-Kdo. Previously it has been suggested that the WahA protein is involved in the incorporation of GlcN residue to outer core lipopolysaccharide (LPS). The WahA protein contains two domains: a glycosyltransferase and a carbohydrate esterase. In this work we demonstrate that the independent expression of the WahA glycosyltransferase domain catalyzes the incorporation of GlcNAc from UDP-GlcNAc to the outer core LPS. Independent expression of the carbohydrate esterase domain leads to the deacetylation of the GlcNAc residue to GlcN. Thus, the WahA is the first described bifunctional glycosyltransfease enzyme involved in the biosynthesis of core LPS. By contrast in Enterobacteriaceae containing GlcN in their outer core LPS the two reactions are performed by two different enzymes
Jimenez N, Lacasta A, Vilches S, Reyes M, Vazquez J, Aquillini E, Merino S, Regue M, Tomas JM Genetics and proteomics of Aeromonas salmonicida lipopolysaccharide core biosynthesis Journal of Bacteriology191(7) (2009)
2228-2236
The structure was elucidated in this paper NCBI PubMed ID:19151135 Publication DOI:10.1128/JB.01395-08 Journal NLM ID:2985120R Publisher: American Society for Microbiology Correspondence: jtomasub.edu Institutions: Departamento de Microbiologia, Facultad de Biologia, Universidad de Barcelona, Diagonal 645, 08071 Barcelona, Spain, Departamento de Microbiologia y Parasitologia Sanitarias, Facultad de Farmacia, Universidad de Barcelona, Av. Joan XXIII s/n, 08028 Barcelona, Spain
Comparison between the lipopolysaccharide (LPS) core structures of Aeromonas salmonicida subsp. salmonicida A450 and Aeromonas hydrophila AH-3 shows great similarity in the inner LPS core and part of the outer LPS core but some differences in the distal part of the outer LPS core (residues ld-Hep, d-Gal, and d-GalNAc). The three genomic regions encoding LPS core biosynthetic genes in A. salmonicida A450, of which regions 2 and 3 have genes identical to those of A. hydrophila AH-3, were fully sequenced. A. salmonicida A450 region 1 showed seven genes: three identical to those of A. hydrophila AH-3, three similar but not identical to those of A. hydrophila AH-3, and one without any homology to any well-characterized gene. A. salmonicida A450 mutants with alterations in the genes that were not identical to those of A. hydrophila AH-3 were constructed, and their LPS core structures were fully elucidated. At the same time, all the A. salmonicida A450 genes identical to those of A. hydrophila AH-3 were used to complement the previously obtained A. hydrophila AH-3 mutants for each of these genes. Combining the gene sequence and complementation test data with the structural data and phenotypic characterization of the mutant LPSs enabled a presumptive assignment of all LPS core biosynthesis gene functions in A. salmonicida A450. Furthermore, hybridization studies with internal probes for the A. salmonicida-specific genes using different A. salmonicida strains (strains of different subspecies or atypical strains) showed a unique or prevalent LPS core type, which is the one fully characterized for A. salmonicida A450.
Banoub JH, El Aneed A, Cohen AM, Joly N Structural investigation of bacterial lipopolysaccharides by mass spectrometry and tandem mass spectrometry Mass Spectrometry Reviews29(4) (2010)
606-650
NCBI PubMed ID:20589944 Publication DOI:10.1002/mas.20258 Journal NLM ID:8219702 Publisher: Wiley Correspondence: joe.banoubdfo-mpo.gc.ca Institutions: Fisheries and Oceans Canada, Science Branch, Special Projects, P.O. Box 5667, St. John's, Newfoundland, Canada A1C 5X1, Department of Chemistry, Memorial University of Newfoundland, St. John's, Newfoundland, Canada A1B 3V6, College of Pharmacy and Nutrition, University of Saskatchewan, Thorvaldson Building, 110 Science Place, Saskatoon, Saskatchewan, Canada S7N 5C9, Unité de Catalyse et de Chimie du Solide, Site de l'Artois—UMR CNRS 8181, I.U.T. de Béthune, Département Chimie, 1230 rue de l'Université, BP819, 62408 Béthune Cedex, France, Institute for Marine Biosciences Room 219A, (NRC-IMB), National Research Council of Canada, Government of Canada, 1411 Oxford Street, Halifax, NS, Canada B3H 3Z1
Mass spectrometric studies are now playing a leading role in the elucidation of lipopolysaccharide (LPS) structures through the characterization of antigenic polysaccharides, core oligosaccharides and lipid A components including LPS genetic modifications. The conventional MS and MS/MS analyses together with CID fragmentation provide additional structural information complementary to the previous analytical experiments, and thus contribute to an integrated strategy for the simultaneous characterization and correct sequencing of the carbohydrate moiety.
LPS, O-antigen, lipid A, core oligosaccharide, MS and MS/MS analyses
Structure type: oligomer Location inside paper: p.632, fig.16 The structure in this paper was incorrect:
Methods: MS/MS, MS Comments, role: review; structure from the original ref. [Banoub et al., 2004b, Eur J Mass Spectrom 10(5):715–730, DOI:10.1255/ejms.673]. Dephosphorylated core oligosaccharide contains 4,8-anhydro and/or 4,7-anhydro derivatives of the enolizable α-keto-acids at the reducing end.
Related record ID(s): 8911 NCBI Taxonomy refs (TaxIDs):29491 Reference(s) to other database(s): GTC:G63005PW Show glycosyltransferases
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