Thiol proteinase expression and pathogenicity of Entamoeba histolytica.

Abstract

Expression of the 56-kilodalton (kDa) neutral thiol proteinase has been shown to correlate with the potential of clinical isolates of Entamoeba histolytica to produce invasive disease. A 56-kDa band was identified by gelatin substrate gel electrophoresis in 10 of 10 isolates from patients with colitis or amebic liver abscesses, but in only 1 of 10 isolates from asymptomatic patients. Pathogenic isolates appear capable of releasing significantly larger quantities of the proteinase, as measured by cleavage of a synthetic peptide substrate, ZRR-AMC (benzyloxy-carbonyl-arginine-arginine-4-amino-7-methylcoumarin). We have also shown that the proteinase is released during the course of clinical invasive amebic disease, as demonstrated by the presence of circulating antibodies detectable by enzyme-linked immunosorbent assay. These studies support the importance of the 56-kDa thiol proteinase in the pathogenesis of invasive amebiasis.

• Authors: S L Reed, W E Keene, J H McKerrow
• Journal: Journal of clinical microbiology (J Clin Microbiol) Vol. 27 Issue 12 Pg. 2772-7 (Dec 1989) ISSN: 0095-1137 [Print] United States
• PMID: 2556432 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't, Research Support, U.S. Gov't, P.H.S.)

Chemical References

• Cysteine Endopeptidases

Topics

• Amebiasis (parasitology)
• Animals
• Cysteine Endopeptidases (analysis, biosynthesis)
• Dysentery, Amebic (parasitology)
• Electrophoresis, Polyacrylamide Gel
• Electrophoresis, Starch Gel
• Entamoeba histolytica (enzymology, pathogenicity)
• Entamoebiasis (parasitology)
• Enzyme-Linked Immunosorbent Assay
• Humans
• Liver Abscess, Amebic (parasitology)