Lysis of erythrocytes by the secreted cysteine proteinase of Porphyromonas gingivalis W83.
The cysteine proteinase produced in the culture supernatant of Porphyromonas gingivalis was extensively purified. Haemagglutination type assays in which the enzyme was titrated against a fixed concentration of erythrocytes, showed that low levels of enzyme directly caused lysis of the red blood cells. However, using the same assay, the presence of stoichiometric amounts of the thiol blocking agent, 2,2'-dipyridyl disulphide (2-PDS) specifically inhibited the action of the enzyme or its haemagglutination with W83 cells or vesicles. In all cases, electron micrographs revealed that in the presence of 2-PDS the erythrocytes remained intact. Thiol activator free enzyme or aerated, inactivated enzyme had no effect on the red blood cells. These results show conclusively that the secreted cysteine proteinase of P. gingivalis causes lysis of erythrocytes and must now be regarded as a potent virulence determinant of P. gingivalis.
Shah
H N
HN
Department of Oral Microbiology, London Hospital Medical College, U.K.
Gharbia
S E
SE
D000818:Animals; D001439:Bacteroides / Q000201:enzymology / Q000378:metabolism*; D003546:Cysteine Endopeptidases / Q000096:biosynthesis* / Q000302:isolation & purification; D004912:Erythrocytes; D006384:Hemagglutination; D006461:Hemolysis; D012756:Sheep
D003546:Cysteine Endopeptidases