Molecular cloning of a cDNA encoding a putative cuticle collagen of Trichinella spiralis § B.Q. Fu a,b , M.Y. Liu a, * , C.M.O. Kapel c , X.P. Meng a , Q. Lu a , X.P. Wu a , Q.J. Chen d , P. Boireau b a Veterinary College, JILIN University, 5333 Xian Road, 130062 Changchun, PR China b UMR 956 INRA-AFSSA-ENVA-UPVM, Biologie Moleculaire et Immunologie Parasitaires et fongiques, 22, rue Pierre Curie, 94703 Maisons-Alfort, France c Danish Centre for Experimental Parasitology, The Royal Veterinary and Agricultural University, Dyrlaegevej 100, DK1870 Frederiksberg C, Denmark d Karolinska Institute, S-17177 Stockholm, Sweden Abstract A 5-day-old adult stage-specific cDNA fragment from Trichinella spiralis was identified by suppression subtractive hybridization and was used as a probe to screen the cDNA library. The cDNA sequence coding for a putative T. spiralis cuticle collagen was isolated. The cDNA encoded an open reading frame of 343 amino acid residues with molecular weight of 35.1 kDa. The deduced protein contained an N-terminal signal peptide, a nematode cuticle collagen N-terminal domain and a collagen triple helix repeat domain. Searches in GenBank using BLASTP showed up to 47% identity to cuticle collagens from other nematodes. Southern blot analysis of genomic DNA indicated this gene was present as a single copy in T. spiralis genome. # 2005 Elsevier B.V. All rights reserved. Keywords: Trichinella spiralis; cDNA; Cuticle collagen 1. Introduction Trichinella spiralis is one of the most widespread parasites and can infect humans and more than 150 species of mammals all over the world. Except for its brief life as a migratory newborn larva (NBL), T. spiralis lives as an intracellular parasite and completes its entire life cycle in the same host. Once in its enteral niche, the infective muscle larvae mature into adult worms within 30 h after four molts and adult females produce newborn larvae from day 5 after infection (Despommier, 1983). The nematode surface includes cuticle, epicuticle and surface coat, and undertakes vital physiological functions (Maizels et al., 1993). The stage-specific surface components and the excretory–secretory (ES) proteins in parasitic nema- todes are the most attractive targets for vaccine development (Maizels et al., 1999) and the nematode www.elsevier.com/locate/vetpar Veterinary Parasitology 132 (2005) 31–35 § The nucleotide sequence data reported in this paper are available in the GenBank database under the accession number AY125953. * Corresponding author. Tel.: +86 431 7998047; fax: +86 431 7998047. E-mail address: liumy36@yahoo.com (M.Y. Liu). 0304-4017/$ – see front matter # 2005 Elsevier B.V. All rights reserved. doi:10.1016/j.vetpar.2005.05.020