Recombinant fragilysin isoforms cause E-cadherin cleavage of intact cells and do not cleave isolated E-cadherin.

Microb Pathog

Scientific Research Institute of Physical-Chemical Medicine of the Federal Medical and Biological Agency, Malaya Pirogovskaya str. 1a, Moscow 119435, Russia; Moscow Institute of Physics and Technology, Institutskiy per. 9, Dolgoprudny, Moscovskaya obl 141700, Russia.

Published: February 2016

The fragilysin (BFT) is a protein secreted by enterotoxigenic Bacteroides fragilis strains. BFT contains zinc-binding motif which was found in the metzincins family of metalloproteinases. In this study, we generated three known recombinant isoforms of BFT using Escherichia coli, tested their activity and examined whether E-cadherin is a substrate for BFTs. BFT treatment of HT-29 cells induced endogenous E-cadherin cleavage, and this BFT activity requires the native structure of zinc-binding motif. At the same time recombinant BFTs did not cleave recombinant E-cadherin or E-cadherin in isolated cell fractions. It indicates that E-cadherin may be not direct substrate for BFT. We also detected and identified proteins released into the cultural medium after HT-29 cells treatment with BFT. The role of these proteins in pathogenesis and cell response to BFT remains to be determined.

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Source
http://dx.doi.org/10.1016/j.micpath.2015.05.003DOI Listing

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