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Journal of Bacteriology, February 2001, p. 942-950, Vol. 183, No. 3
0021-9193/01/$04.00+0   DOI: 10.1128/JB.183.3.942-950.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Structural and Immunochemical Characterization of the Lipooligosaccharides Expressed by Neisseria subflava 44

Yanhong Tong, Vernon Reinhold,dagger Bruce Reinhold,dagger Brenda Brandt,Dagger and Daniel C. Stein*

Department of Cell Biology and Molecular Genetics, University of Maryland, College Park, Maryland 20742

Received 12 July 2000/Accepted 17 October 2000

Neisserial lipooligosaccharides (LOSs) are a family of complex cell surface glycolipids. We used mass spectrometry techniques (electrospray ionization, collision-induced dissociation, and multiple step), combined with fluorophore-assisted carbohydrate electrophoresis monosaccharide composition analysis, to determine the structure of the two low-molecular-mass LOS molecules (LOSI and LOSII) expressed by Neisseria subflava 44. We determined that LOSI contains one glucose on both the alpha  and beta  chains. LOSII is structurally related to LOSI and differs from it by the addition of a hexose (either glucose or galactose) on the alpha  chain. LOSI and LOSII were able to bind monoclonal antibody (MAb) 25-1-LC1 when analyzed by Western blotting experiments. We used a set of genetically defined Neisseria gonorrhoeae mutants that expressed single defined LOS epitopes and a group of Neisseria meningitidis strains that expresses chemically defined LOS components to determine the structures recognized by MAb 25-1-LC1. We found that extensions onto the beta -chain glucose of LOSI block the recognition by this MAb, as does further elongation from the LOSII alpha  chain. The LOSI structure was determined to be the minimum structure that is recognized by MAb 25-1-LC1.

* Corresponding author. Mailing address: Department of Cell Biology and Molecular Genetics, University of Maryland, College Park, MD 20742. Phone: (301) 405-5448. Fax: (301) 314-9489. E-mail: DS64{at}UMAIL.UMD.EDU.

dagger Present address: Department of Chemistry, University of New Hampshire. Durham, NH 03824.

Dagger Present address: Walter Reed Army Institute of Research, Department of Bacterial Diseases, Division of Communicable Diseases and Immunology, Silver Spring, MD 20910.

Journal of Bacteriology, February 2001, p. 942-950, Vol. 183, No. 3
0021-9193/01/$04.00+0   DOI: 10.1128/JB.183.3.942-950.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:

  • O'Connor, E. T., Piekarowicz, A., Swanson, K. V., Griffiss, J. M., Stein, D. C. (2006). Biochemical Analysis of Lpt3, a Protein Responsible for Phosphoethanolamine Addition to Lipooligosaccharide of Pathogenic Neisseria. J. Bacteriol. 188: 1039-1048 [Abstract] [Full Text]  
  • Braun, D. C., Stein, D. C. (2004). The lgtABCDE Gene Cluster, Involved in Lipooligosaccharide Biosynthesis in Neisseria gonorrhoeae, Contains Multiple Promoter Sequences. J. Bacteriol. 186: 1038-1049 [Abstract] [Full Text]  
  • Piekarowicz, A., Stein, D. C. (2002). Biochemical Properties of Neisseria gonorrhoeae LgtE. J. Bacteriol. 184: 6410-6416 [Abstract] [Full Text]  
  • Tong, Y., Arking, D., Ye, S., Reinhold, B., Reinhold, V., Stein, D. C. (2002). Neisseria gonorrhoeaestrain PID2 simultaneously expresses six chemically related lipooligosaccharide structures. Glycobiology 12: 523-533 [Abstract] [Full Text]  
  • Arking, D., Tong, Y., Stein, D. C. (2001). Analysis of Lipooligosaccharide Biosynthesis in the Neisseriaceae. J. Bacteriol. 183: 934-941 [Abstract] [Full Text]  


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