Helmholtz Gemeinschaft

Search
Browse
Statistics
Feeds

Isolation and molecular characterization of a surface-bound proteinase of Entamoeba histolytica

Item Type:Article
Title:Isolation and molecular characterization of a surface-bound proteinase of Entamoeba histolytica
Creators Name:Jacobs, T. and Bruchhaus, I. and Dandekar, T. and Tannich, E. and Leippe, M.
Abstract:Major pathogenic functions of Entamoeba histolytica involved in destruction of host tissues are the degradation of extracellular matrix proteins mediated by secreted cysteine proteinases and contact-dependent killing of host cells via membrane-active factors. A soluble protein with an affinity for membranes was purified from amoebic extracts to apparent homogeneity. N-terminal sequencing and subsequent molecular cloning of the factor revealed that it is a member of the cysteine proteinase family of E. histolytica, which we termed CP5. Further experiments with the purified protein showed that it has potent proteolytic activity that is abrogated in the presence of inhibitors specific for cysteine proteinases. The enzyme firmly associates with membranes retaining its proteolytic activity and it produces cytopathic effects on cultured monolayers. A model of the three-dimensional structure of CP5 revealed the presence of a hydrophobic patch that may account for the potential of the protein to associate with membranes. Immunocytochemical localization of the enzyme to the surface of the amoeba in combination with the recent finding that the gene encoding CP5 is missing in the closely related but non-pathogenic Entamoeba dispar suggests a potential role of the protein in host tissue destruction of E. histolytica.
Keywords:Amino Acid Sequence, Base Sequence, Cysteine Endopeptidases, Protozoan DNA, Entamoeba Histolytica, Membrane Proteins, Molecular Models, Molecular Sequence Data, Protein Conformation, Animals, Rabbits
Source:Molecular Microbiology
ISSN:0950-382X
Publisher:Blackwell (U.K.)
Volume:27
Number:2
Page Range:269-276
Date:January 1998
Official Publication:https://doi.org/10.1046/j.1365-2958.1998.00662.x
PubMed:View item in PubMed

Repository Staff Only: item control page

Open Access
MDC Library