NDLI: Cloning and analysis of a cDNA encoding a putative serine protease comprising two trypsin-like domains of Trichinella spiralis

Content Provider	Springer Nature Link
Author	Trap, Catherine Fu, Baoquan Guerhier, Franck Liu, Mingyuan Rhun, Danielle Romand, Thibault Perret, Catherine Blaga, Radu Boireau, Pascal
Copyright Year	2005
Abstract	The cDNA encoding a putative serine protease, TsSerP, was cloned by degenerative polymerase chain reaction and screening of the cDNA library from Trichinella spiralis adult–newborn larvae stage. Sequence analysis revealed the presence of two trypsin-like serine protease domains flanking a hydrophilic domain, with the catalytic triad residue histidine in the alpha domain substituted by an arginine residue. Southern blots indicated that this was a single copy gene in the parasite genome. Northern blots demonstrated a single 2.3-kb transcript during the muscle larvae and adult stages of T. spiralis. The recombinant protein from the TsSerP beta domain (βSerP) was produced but not recognised by T. spiralis-infected swine serum. An anti-βSerP polyclonal serum detected a 69-kDa polypeptide in the soluble antigens of T. spiralis muscle larvae. Immunolocalisation analysis located TsSerP on the inner layer of the cuticle and oesophagus of the parasite, suggesting a potential role in its moulting and/or digestive functions.
Starting Page	288
Ending Page	294
Page Count	7
File Format	PDF
ISSN	09320113
Journal	Parasitology Research
Volume Number	98
Issue Number	4
e-ISSN	14321955
Language	English
Publisher	Springer-Verlag
Publisher Date	2005-12-10
Publisher Place	Berlin/Heidelberg
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Trichinella spiralis Serine protease Trypsin-like domain cDNA library Cloning Immunology Microbiology Medical Microbiology
Content Type	Text
Resource Type	Article
Subject	Infectious Diseases Veterinary Parasitology Insect Science

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