Molecular characterisation of a protective, 11-kDa excretory-secretory protein from the parasitic stages of Trichostrongylus colubriformis.
An 11-kDa protein occurring as a major component of the non-glycosylated fraction of 4th larval stage (L4) and adult Trichostrongylus colubriformis excretory-secretory (ES) fluid has been found to be highly protective in guinea pigs, an alternate host for T. colubriformis. The protein has been purified, characterised and partly sequenced. With a reverse-complement oligonucleotide based on the carboxy-terminal sequence of the protein, recombinant lambda gt11 clones were detected in an L4 cDNA library. The DNA sequence from one clone has a single extended open reading frame coding for a highly charged 11-kDa protein which lacks a leader sequence and contains a potential N-glycosylation site. Expression of the cloned DNA in Escherichia coli was detected with an antibody, raised in rabbits against gel-purified 11-kDa protein.
Dopheide
T A
TA
Division of Biomolecular Engineering, CSIRO, Parkville Laboratory, Victoria, Australia.
Tachedjian
M
M
Phillips
C
C
Frenkel
M J
MJ
Wagland
B M
BM
Ward
C W
CW
D000595:Amino Acid Sequence; D000818:Animals; D000947:Antigens, Helminth / Q000096:biosynthesis / Q000235:genetics*; D001483:Base Sequence; D015152:Blotting, Northern; D003001:Cloning, Molecular; D004247:DNA / Q000737:chemistry; D004926:Escherichia coli / Q000235:genetics; D015870:Gene Expression; D006031:Glycosylation; D006168:Guinea Pigs; D015801:Helminth Proteins / Q000096:biosynthesis / Q000235:genetics*; D008969:Molecular Sequence Data; D008970:Molecular Weight; D012313:RNA / Q000737:chemistry; D012689:Sequence Homology, Nucleic Acid; D014254:Trichostrongylus / Q000235:genetics*
D000947:Antigens, Helminth; D015801:Helminth Proteins; C069376:excretory-secretory protein 11 kDa, Trichostrongylus colubriformis; D012313:RNA; D004247:DNA