Activation of the Human Complement Cascade by Bacterial Cell Walls, Peptidoglycans, Water-Soluble Peptidoglycan Components, and Synthetic Muramylpeptides Studies on Active Components and Structural Requirements

Akinori Kawasaki, Shinya Inai, Kazuyoshi Nagaki, Misako Matsumoto, Haruhiko Takada, Shozo Kotani, Kanae Yokogawa, Shigeo Kawata, Shoichi Kusumoto, Tetsuo Shiba

Research output: Contribution to journalArticlepeer-review

25 Citations (Scopus)

Abstract

Cell walls isolated from 29 strains of 24 gram-positive bacterial species, whose peptidoglycans belong to the group A type of Schleifer and Kandler's classification, with one exception (Arthrobacter sp.), were shown to activate the complement cascade in pooled fresh human serum mainly through the alternative pathway and partly through the classical one. The complement-activating effect of cell walls (5 species) possessing group B type peptidoglycan, except those of Corynebacterium insidiosum, was weaker than that of the walls with group A type peptidoglycan. Preparations of peptidoglycan isolated from cell walls of Staphylococcus aureus, Streptococcus pyogenes, and Lactobacillus plantarum also activated the alternative pathway of the complement cascade, but less effectively than the respective parent cell walls. A water-soluble “polymer” of peptidoglycan subunits (SEPS), which was prepared from Staphylococcus epidermidis peptidoglycans by treatment with a cross-bridge degrading endopeptidase, retained most of the complement-activating ability of the parent cell walls. A peptidoglycan “monomer,” SEPS-M, which was obtained by hydrolysis of the glycan chain of SEPS with endo-N-acetylmuramidase to disaccharide units did not activate complement. In conformity with this finding, neither synthetic N-acetylmuramyl-L-alanyl-D-isoglutamine (MDP) nor MDP-L-Lys-D-Ala activated the complement cascade. Among several lipophilic derivatives of MDP, 6-O-(3-hydroxy-3 - docosylhexacosanoyl) - MDP-L-Lys-D-Ala (BH48-MDP-L-Lys-D-Ala) and 6-O- (2-tetradecylhexadecanoy 1)-MDP (B30-MDP) were shown to activate complement through the alternative as well as the classical pathway and exclusively through the classical pathway, respectively. The finding that a D-isoasparagine.

Original languageEnglish
Pages (from-to)551-569
Number of pages19
JournalMICROBIOLOGY and IMMUNOLOGY
Volume31
Issue number6
DOIs
Publication statusPublished - 1987 Jan 1

ASJC Scopus subject areas

  • Microbiology
  • Immunology
  • Virology

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