Structure of Campylobacter jejuni Lipopolysaccharides Determines Antiganglioside Specificity and Clinical Features of Guillain-Barré and Miller Fisher Patients
Author:
Affiliation:
1. Departments of Neurology
2. Immunology
3. Microbiology and Infectious Diseases, Erasmus University/Academic Hospital Dijkzigt Rotterdam, Rotterdam, The Netherlands
4. Department of Neurology, Southern General Hospital, Glasgow G51 4TF, Scotland
Abstract
Publisher
American Society for Microbiology
Subject
Infectious Diseases,Immunology,Microbiology,Parasitology
Link
https://journals.asm.org/doi/pdf/10.1128/IAI.70.3.1202-1208.2002
Reference37 articles.
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2. Ang, C. W., N. Yuki, B. C. Jacobs, M. Koga, P. A. Van Doorn, P. I. M. Schmitz, and F. G. A. Van Der Meché. 1999. Rapidly progressive, predominantly motor Guillain-Barré syndrome with anti-GalNAc-GD1a antibodies. Neurology53:2122-2127.
3. Angstrom, J., S. Teneberg, and K. A. Karlsson. 1994. Delineation and comparison of ganglioside-binding epitopes for the toxins of Vibrio cholerae, Escherichia coli, and Clostridium tetani: evidence for overlapping epitopes. Proc. Natl. Acad. Sci. USA91:11859-11863.
4. Asbury, A. K., and D. R. Cornblath. 1990. Assessment of current diagnostic criteria for Guillain-Barré syndrome. Ann. Neurol.27:S21-S24.
5. Lipopolysaccharides from Campylobacter jejuni associated with Guillain-Barré syndrome patients mimic human gangliosides in structure
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