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© Research
Publication : Nature communications

The parasite Entamoeba histolytica exploits the activities of human matrix metalloproteinases to invade colonic tissue

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Nature communications - 07 Oct 2014

Thibeaux R, Avé P, Bernier M, Morcelet M, Frileux P, Guillén N, Labruyère E

Link to Pubmed [PMID] – 25291063

Nat Commun 2014;5:5142

Intestinal invasion by the protozoan parasite Entamoeba histolytica is characterized by remodelling of the extracellular matrix (ECM). The parasite cysteine proteinase A5 (CP-A5) is thought to cooperate with human matrix metalloproteinases (MMPs) involved in ECM degradation. Here, we investigate the role CP-A5 plays in the regulation of MMPs upon mucosal invasion. We use human colon explants to determine whether CP-A5 activates human MMPs. Inhibition of the MMPs’ proteolytic activities abolishes remodelling of the fibrillar collagen structure and prevents trophozoite invasion of the mucosa. In the presence of trophozoites, MMPs-1 and -3 are overexpressed and are associated with fibrillar collagen remodelling. In vitro, CP-A5 performs the catalytic cleavage needed to activate pro-MMP-3, which in turn activates pro-MMP-1. Ex vivo, incubation with recombinant CP-A5 was enough to rescue CP-A5-defective trophozoites. Our results suggest that MMP-3 and/or CP-A5 inhibitors may be of value in further studies aiming to treat intestinal amoebiasis.

http://www.ncbi.nlm.nih.gov/pubmed/25291063