Molecular characterisation of a protective, 11-kDa excretory-secretory protein from the parasitic stages of Trichostrongylus colubriformis

• Published in: Molecular and biochemical parasitology Vol. 45; no. 1; pp. 101 - 107
• Main Authors: Dopheide, Theo A.A., Tachedjian, Mary, Phillips, Clare, Frenkel, Maurice J., Wagland, Barry M., Ward, Colin W.
• Format: Journal Article
• Language: English
• Published: Shannon Elsevier B.V 01.03.1991; Elsevier Science
• Subjects: Amino Acid Sequence; amino acid sequences; Animals; Antigens, Helminth - biosynthesis; Antigens, Helminth - genetics; Base Sequence; Biochemistry. Physiology. Immunology. Molecular biology; Biological and medical sciences; Blotting, Northern; clones; Cloning, Molecular; DNA; DNA - chemistry; Escherichia coli - genetics; Excretory-secretory; Fundamental and applied biological sciences. Psychology; genbank/m38527; Gene Expression; Glycosylation; Guinea Pigs; Helminth Proteins - biosynthesis; Helminth Proteins - genetics; Host protection; Invertebrates; Molecular Sequence Data; Molecular Weight; molecularl sequence data; Nemathelminthia. Plathelmintha; nucleotide sequences; Physiology. Development; proteins; RNA - chemistry; Sequence Homology, Nucleic Acid; sheep; Trichostrongylus - genetics; Trichostrongylus colubriformis; Excretory-secretory; SDS; TBS; Host protection; IPTG; PAGE; Trichostrongylus colubriformis; ES; TFA; Biological properties; Host parasite relation; Purification; Rodentia; Host; Characterization; Northern blotting; Proteins; Vertebrata; Mammalia; Guinea pig; Complementary DNA; Helmintha; Nemathelminthia; Developmental stage; Invertebrata; Molecular cloning; Nematoda; Protection
• ISSN: 0166-6851; 1872-9428
• DOI: 10.1016/0166-6851(91)90031-Z

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 λgt11 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.