This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow E-mail this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in ASM journals
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Moore, S. L.
Right arrow Articles by Michon, F.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Moore, S. L.
Right arrow Articles by Michon, F.

 Previous Article  |  Next Article 

Clinical and Vaccine Immunology, October 2007, p. 1311-1317, Vol. 14, No. 10
1071-412X/07/$08.00+0     doi:10.1128/CVI.00049-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

Epitope Specificities of the Group Y and W-135 Polysaccharides of Neisseria meningitidis{triangledown}

Samuel L. Moore,1* Catherine Uitz,2 Chang-Chun Ling,3 David R. Bundle,3 Peter C. Fusco,1 and Francis Michon1*

Wellstat Vaccines, 9 West Watkins Mill Road, Gaithersburg, Maryland 20878,1 Emergent Biosolutions, 300 Professional Drive, Gaithersburg, Maryland 20879,2 Alberta Ingenuity Centre for Carbohydrate Science, Department of Chemistry, University of Alberta, Edmonton, Alberta T6G 2G2, Canada3

Received 24 January 2007/ Returned for modification 27 April 2007/ Accepted 22 August 2007

Previous studies have identified the length dependency of several polysaccharide (PS) protective epitopes. We have investigated whether meningococcal polysaccharides Y and W-135 possess such epitopes. Oligosaccharides (OSs) consisting of one or more disaccharide repeating units (RU) were derived from the capsular PSs of group Y and W-135 meningococci (GYMP and GWMP, respectively) by mild acid hydrolysis. The relative affinities of anticapsular antibodies binding to derivative OSs of different chain lengths were measured in inhibition enzyme-linked immunosorbent assays. As OS size increased from two to three RU, there was a notable increase in binding inhibition of rabbit anti-group Y antiserum. This pattern of antibody binding inhibition was also observed for rabbit antiserum to group W-135, though the inhibition increase was much more pronounced. In the cases of both OS species, the concentration of inhibiting antigen required to achieve 50% inhibition of rabbit immunoglobulin binding increased progressively as the inhibiting disaccharide chain length increased from 1 RU through greater than 50 RU. These data suggest that antibodies directed against both of these meningococcal PSs recognize conformational epitopes only fully expressed in higher-molecular-weight forms of these antigens.

* Corresponding author. Mailing address: Department of Vaccine Research, Wellstat Vaccines, 9 West Watkins Mill Rd., Gaithersburg, MD 20878. Phone: (301) 519-7079. Fax: (301) 519-7117. E-mail for S. L. Moore: smoore{at}wellstatdiagnostics.com. E-mail for F. Michon: fmichon{at}wellstatvaccines.com

{triangledown} Published ahead of print on 5 September 2007.

Clinical and Vaccine Immunology, October 2007, p. 1311-1317, Vol. 14, No. 10
1071-412X/07/$08.00+0     doi:10.1128/CVI.00049-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.





Copyright © 2010 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»