Molecular cloning of a cDNA encoding a putative cuticle collagen of Trichinella spiralis.
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 k Da. 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.
Veterinary College, JILIN University, 5333 Xian Road, 130062 Changchun, PR China.
B Q
BQ
Fu
M Y
MY
Liu
C M O
CM
Kapel
X P
XP
Meng
Q
Q
Lu
X P
XP
Wu
Q J
QJ
Chen
P
P
Boireau
D000595:Amino Acid Sequence; D000818:Animals; D015139:Blotting, Southern; D015153:Blotting, Western; D003001:Cloning, Molecular; D003094:Collagen / Q000235:genetics*; D015723:Gene Library; D008969:Molecular Sequence Data; D009693:Nucleic Acid Hybridization; D018510:RNA, Helminth / Q000737:chemistry / Q000235:genetics; D011994:Recombinant Proteins / Q000235:genetics; D020133:Reverse Transcriptase Polymerase Chain Reaction; D017160:Trichinella spiralis / Q000235:genetics*
D018510:RNA, Helminth; D011994:Recombinant Proteins; D003094:Collagen