Cloning and analysis of a novel cDNA from Trichinella spiralis encoding a protein with an FYVE zinc finger domain.
A cDNA library from Trichinella spiralis adults 3 days post-infection was screened with a cDNA probe, designated T 54, derived from a newborn larvae subtracted cDNA library. Sequence analysis showed that the positive clone contained a cDNA insert of 1464 bp in length with a single open reading frame of 1290 bp, which encoded a protein of 429 amino acids with a putative molecular mass of 49.9 k Da. Database analysis predicted the deduced protein had a leucine zipper motif and an FYVE zinc finger domain. The recombinant fusion protein was expressed and rabbit anti-recombinant protein sera reacted with a single peptide migrating at approximately 55 k Da in crude worm extract from muscle larvae, adults and newborn larvae stages.
Fu
B Q
BQ
Veterinary College, JILIN University, 5333 Xian Road, 130062 Changchun, PR China.
Liu
M Y
MY
Kapel
C M O
CM
Meng
X P
XP
Lu
Q
Q
Wu
X P
XP
Chen
Q J
QJ
Boireau
P
P
D000595:Amino Acid Sequence; D000818:Animals; D015153:Blotting, Western; D003001:Cloning, Molecular; D018076:DNA, Complementary / Q000737:chemistry / Q000235:genetics; D015723:Gene Library; D016350:Leucine Zippers / Q000235:genetics; D051379:Mice; D008969:Molecular Sequence Data; D009693:Nucleic Acid Hybridization; D051381:Rats; D011994:Recombinant Proteins / Q000235:genetics; D017160:Trichinella spiralis / Q000235:genetics* / Q000302:isolation & purification; D014235:Trichinellosis / Q000469:parasitology; D016335:Zinc Fingers / Q000235:genetics*
D018076:DNA, Complementary; D011994:Recombinant Proteins