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Title: Molecular cloning and characterization of serine protease inhibitor from food-borne nematode, Gnathostoma spinigerum
Authors: Anusorn Tinyou
Salisa Chaimon
Orawan Phuphisut
Porntida Kobpornchai
Preeyarat Malaithong
Akkarin Poodeepiyasawat
Issariya Ieamsuwan
Jiraporn Ruangsittichai
Pornpan Pumirat
Paron Dekumyoy
Onrapak Reamtong
Poom Adisakwattana
Huachiew Chalermprakiet University
Mahidol University
Keywords: Agricultural and Biological Sciences;Immunology and Microbiology;Medicine;Veterinary
Issue Date: 1-Apr-2020
Citation: Acta Tropica. Vol.204, (2020)
Abstract: © 2019 Elsevier B.V. Gnathostoma spinigerum is a causative agent of human gnathostomiasis and infects people residing in endemic areas as well as travelers. Cutaneous and visceral larval migrants cause clinical manifestations, resulting in severe morbidity and mortality. To survive in hosts, these parasites have evolved various immune evasion mechanisms, including the release of regulatory molecules. Serine protease inhibitors (serpins) that are present in many parasitic helminths are proteins suspected of suppressing host serine protease-related digestion and immune responses. In this study, the serpin secreted by G. spinigerum (GsSerp) was characterized using bioinformatics and molecular biology techniques. The bioinformatics revealed that GsSerp contains 9 helices, 3 β-sheets, and a reactive central loop, which are conserved structures of the serpin superfamily. Recombinant GsSerp (rGsSerp) was expressed in E. coli (molecular weight, 39 kDa) and could inhibit chymotrypsin. Mouse polyclonal antibody against GsSerp could detect the native GsSerp in crude worm antigen but not the excretory–secretory product (ES) of infective-stage larva (aL3Gs). Moreover, the expression of GsSerp in the aL3Gs tissue was located in the hemolymph and intestinal tissue, indicating its role in parasite homeostasis. Our findings may help develop effective strategies for preventing and controlling gnathostomiasis.
ISSN: 18736254
Appears in Collections:Scopus 2020

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