Preparation of arthritogenic hydrosoluble peptidoglycans from both arthritogenic and non-arthritogenic bacterial cell walls.

Abstract

Cell wall lytic enzyme (Kyowa lytic no. 2 enzyme) liberated arthritogenic hydrosoluble peptidoglycans from both arthritogenic and non-arthritogenic bacterial cell walls. From these cell walls, mutanolysin (peptidoglycan-degrading enzyme) also liberated hydrosoluble peptidoglycans which, however, lacked arthritogenicity. Based on the chemical composition of these peptidoglycans, it was suggested that their arthritis-inducing ability depends on a relatively long chain of glycan units that consists of repeated units of N-acetylglucosaminyl-N-acetylmuramic acid. However, the glycan chain lengths on these peptidoglycans appeared to be related to their adjuvancy rather than to an antigen(s) responsible for development of arthritis in rats.

• Authors: O Kohashi, C M Pearson, Y Watanabe, S Kotani
• Journal: Infection and immunity (Infect Immun) Vol. 16 Issue 3 Pg. 861-6 (Jun 1977) ISSN: 0019-9567 [Print] United States
• PMID: 302240 (Publication Type: Comparative Study, Journal Article, Research Support, U.S. Gov't, P.H.S.)

Chemical References

• Peptidoglycan
• Water
• Squalene
• Endopeptidases
• Kyowa lytic no. 2 enzyme
• mutanolysin

Topics

• Animals
• Arthritis, Experimental (chemically induced)
• Bacteria (analysis)
• Cell Wall (analysis, metabolism)
• Endopeptidases (metabolism)
• Female
• Hypersensitivity, Delayed (chemically induced)
• Peptidoglycan (adverse effects, isolation & purification, metabolism)
• Rats
• Rats, Inbred Lew
• Solubility
• Species Specificity
• Squalene
• Water