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Research Article Free access | 10.1172/JCI116565

A structure-activity relationship for induction of meningeal inflammation by muramyl peptides.

M Burroughs, E Rozdzinski, S Geelen, and E Tuomanen

Laboratory of Molecular Infectious Diseases, Rockefeller University, New York 10021.

Find articles by Burroughs, M. in: PubMed | Google Scholar

Laboratory of Molecular Infectious Diseases, Rockefeller University, New York 10021.

Find articles by Rozdzinski, E. in: PubMed | Google Scholar

Laboratory of Molecular Infectious Diseases, Rockefeller University, New York 10021.

Find articles by Geelen, S. in: PubMed | Google Scholar

Laboratory of Molecular Infectious Diseases, Rockefeller University, New York 10021.

Find articles by Tuomanen, E. in: PubMed | Google Scholar

Published July 1, 1993 - More info

Published in Volume 92, Issue 1 on July 1, 1993
J Clin Invest. 1993;92(1):297–302. https://doi.org/10.1172/JCI116565.
© 1993 The American Society for Clinical Investigation
Published July 1, 1993 - Version history
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Abstract

Components of bacterial peptidoglycans have potent biological activities, including adjuvant effects, cytotoxicity, and induction of sleep. Mixtures of peptidoglycan components also induce inflammation in the lung, subarachnoid space, and joint, but the structural requirements for activity are unknown. Using a rabbit model for meningitis, we determined the biological activities of 14 individual muramyl peptides constituting > 90% of the peptidoglycan of the gram-negative pediatric pathogen Haemophilus influenzae. Upon intracisternal inoculation, most of the muropeptides induced leukocytosis in cerebrospinal fluid (CSF), influx of protein into CSF, or brain edema, alone or in combination. The disaccharide-tetrapeptide, the major component of all gram-negative peptidoglycans, induced CSF leukocytosis and protein influx at doses as low as 0.4 microgram (0.42 nM). Modification of the N-acetyl muramic acid or substitution of the alanine at position four in the peptide side chain decreased leukocytosis but enhanced brain edema. As the size of the muropeptide increased, the inflammatory activity decreased. Muropeptide carrying the diaminopimelyl-diaminopimelic acid cross-link specifically induced cytotoxic brain edema. These findings significantly expand the spectrum of biological activities of natural muramyl peptides and provide the basis for a structure-activity relationship for the inflammatory properties of bacterial muropeptides.

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