Purification of a chymotrypsin-like enzyme present on adult Schistosoma mansoni worms from infected mice and its characterization as a host carboxylesterase

Igetei, Joseph E. and Liddell, Susan and El-Faham, Marwa and Doenhoff, Michael J. (2016) Purification of a chymotrypsin-like enzyme present on adult Schistosoma mansoni worms from infected mice and its characterization as a host carboxylesterase. Parasitology, 143 (5). pp. 646-657. ISSN 1469-8161

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Abstract

A serine protease-like enzyme found in detergent extracts of Schistosoma mansoni adult worms perfused from infected mice has been purified from mouse blood and further characterized. The enzyme is approximately 85 kDa and hydrolyses N-acetyl-DL-phenylalanine β-naphthyl–ester, a chromogenic substrate for chymotrypsin-like enzymes. The enzyme from S. mansoni worms appears to be antigenically and enzymatically similar to a molecule that is present in normal mouse blood and so is seemingly host-derived. The enzyme was partially purified by depleting normal mouse serum of albumin using sodium chloride and cold ethanol, followed by repeated rounds of purification by one-dimensional sodium dodecyl sulphate polyacrylamide gel electrophoresis. The purified material was subjected to tandem mass spectrometry and its derived peptides found to belong to mouse carboxylesterase 1C. Its ability to hydrolyse α- or β-naphthyl acetates, which are general esterase substrates, has been confirmed. A similar carboxylesterase was purified and characterized from rat blood. Additional evidence to support identification of the enzyme as a carboxylesterase has been provided. Possible roles of the enzyme in the mouse host–parasite relationship could be to ease the passage of worms through the host's blood vessels and/or in immune evasion.

Item Type: Article
Additional Information: Copyright Cambridge University Press.
Keywords: S. mansoni, host-derived enzyme, mice, carboxylesterase 1C, immune evasion
Schools/Departments: University of Nottingham UK Campus > Faculty of Science > School of Biosciences
University of Nottingham UK Campus > Faculty of Medicine and Health Sciences > School of Life Sciences
Identification Number: https://doi.org/10.1017/S0031182016000184
Depositing User: Eprints, Support
Date Deposited: 10 Feb 2016 15:09
Last Modified: 15 Sep 2016 07:54
URI: http://eprints.nottingham.ac.uk/id/eprint/31612

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