Production of hydrolytic enzymes by oral isolates of Eikenella corrodens.
Eikenella corrodens isolates from periodontally healthy subjects and adult periodontitis patients were compared for their ability to produce a range of potential virulence factors. All were positive for proline aminopeptidase, thiol-dependent haemolysin and esterase activities. Low or negative activities were found against casein, phospholipid, lipid, collagen, aminophosphate, phosphate under acid or alkaline conditions, and eleven other amino acid substrates tested. In oral infections, the haemolytic activity of E. corrodens could be amplified in the reduced environment of the periodontal pocket and damage host cells. Proline aminopeptidase may act against proline residues in collagen, immunoglobulins and complement proteins.
Allaker
R P
RP
Department of Oral Microbiology, London Hospital Medical College, UK.
Young
K A
KA
Hardie
J M
JM
D000328:Adult; D000626:Aminopeptidases / Q000096:biosynthesis; D016124:Eikenella corrodens / Q000201:enzymology* / Q000302:isolation & purification; D004950:Esterases / Q000096:biosynthesis; D006460:Hemolysin Proteins / Q000096:biosynthesis; D006801:Humans; D010518:Periodontitis / Q000382:microbiology*
D006460:Hemolysin Proteins; D004950:Esterases; D000626:Aminopeptidases; C022450:prolyl aminopeptidase