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Please use this identifier to cite or link to this item: http://repository.li.mahidol.ac.th/dspace/handle/123456789/43554
Title: Molecular characterization of serine protease inhibitor isoform 3, SmSPI, from Schistosoma mansoni
Authors: Pattarakul Pakchotanon
Patamaporn Molee
Supaporn Nuamtanong
Yanin Limpanont
Phiraphol Chusongsang
Jareemate Limsomboon
Yupa Chusongsang
Santi Maneewatchararangsri
Urai Chaisri
Poom Adisakwattana
Mahidol University
Keywords: Agricultural and Biological Sciences;Immunology and Microbiology;Medicine
Issue Date: 1-Aug-2016
Citation: Parasitology Research. Vol.115, No.8 (2016), 2981-2994
Abstract: © 2016, Springer-Verlag Berlin Heidelberg. Serine protease inhibitors, known as serpins, are pleiotropic regulators of endogenous and exogenous proteases, and molecule transporters. They have been documented in animals, plants, fungi, bacteria, and viruses; here, we characterize a serpin from the trematode platyhelminth Schistosoma mansoni. At least eight serpins have been found in the genome of S. mansoni, but only two have characterized molecular properties and functions. Here, the function of S. mansoni serpin isoform 3 (SmSPI) was analyzed, using both computational and molecular biological approaches. Phylogenetic analysis showed that SmSPI was closely related to Schistosoma haematobium serpin and Schistosoma japonicum serpin B10. Structure determined in silico confirmed that SmSPI belonged to the serpin superfamily, containing nine α-helices, three β-sheets, and a reactive central loop. SmSPI was highly expressed in schistosomules, predominantly in the head gland, and in adult male and female with intensive accumulation on the spines, which suggests that it may have a role in facilitating intradermal and intravenous survival. Recombinant SmSPI was overexpressed in Escherichia coli; the recombinant protein was of the same size (46 kDa) as the native protein. Immunological analysis suggested that mice infected with S. mansoni responded to rSmSPI at 8 weeks postinfection (wpi) but not earlier. The inhibitory activity of rSmSPI was specific to chymotrypsin but not trypsin, neutrophil elastase, and porcine pancreatic elastase. Elucidating the biological and physiological functions of SmSPI as well as other serpins will lead to further understanding of host-parasite interaction machinery that may provide novel strategies to prevent and control schistosomiasis in the future.
URI: https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=84963736618&origin=inward
http://repository.li.mahidol.ac.th/dspace/handle/123456789/43554
ISSN: 14321955
09320113
Appears in Collections:Scopus 2016-2017

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