rdf:type |
|
lifeskim:mentions |
|
pubmed:issue |
2
|
pubmed:dateCreated |
1991-7-1
|
pubmed:databankReference |
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M37729,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M54897,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M64242,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M64245,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M90695,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/S78945,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/S78946,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/S78947,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/S78948,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/S78949,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/S78950
|
pubmed:abstractText |
Complementary DNA (cDNA) encoding a 49-kDa antigen of Trichinella spiralis was cloned, characterized, and expressed in Escherichia coli by recombinant DNA methods. As a first step, 29 residues of N-terminal amino acid sequence were determined by direct analysis of highly purified antigen. Mixed-sequence primers based on the amino acid sequence were then synthesized and used as primers to generate a partial cDNA by the polymerase chain reaction (PCR). A nearly full-length cDNA was then obtained by PCR using a specific 5'-end primer and a non-specific 3'-end primer. Complete sequence of the 1133-bp cDNA was determined. Translation of this sequence predicts an N-glycosylated polypeptide of 322 amino acids. The cDNA was expressed as a fusion protein in bacteria which could be recognized in Western blots both by sera from mice immunized with purified native 49-kDa antigen and by sera from swine infected with the parasite. These findings suggest that recombinant P49 is a potentially valuable antigen both for vaccine development and immunodiagnosis.
|
pubmed:language |
eng
|
pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
|
pubmed:status |
MEDLINE
|
pubmed:month |
Apr
|
pubmed:issn |
0166-6851
|
pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:volume |
45
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
331-6
|
pubmed:dateRevised |
2006-11-15
|
pubmed:meshHeading |
pubmed-meshheading:2038363-Amino Acid Sequence,
pubmed-meshheading:2038363-Animals,
pubmed-meshheading:2038363-Antigens, Helminth,
pubmed-meshheading:2038363-Base Sequence,
pubmed-meshheading:2038363-Blotting, Western,
pubmed-meshheading:2038363-Cloning, Molecular,
pubmed-meshheading:2038363-DNA,
pubmed-meshheading:2038363-DNA, Single-Stranded,
pubmed-meshheading:2038363-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:2038363-Gene Expression,
pubmed-meshheading:2038363-Glycopeptides,
pubmed-meshheading:2038363-Humans,
pubmed-meshheading:2038363-Mice,
pubmed-meshheading:2038363-Molecular Sequence Data,
pubmed-meshheading:2038363-Oligodeoxyribonucleotides,
pubmed-meshheading:2038363-Polymerase Chain Reaction,
pubmed-meshheading:2038363-Recombinant Fusion Proteins,
pubmed-meshheading:2038363-Swine,
pubmed-meshheading:2038363-Trichinella
|
pubmed:year |
1991
|
pubmed:articleTitle |
Cloning and expression of complementary DNA encoding an antigen of Trichinella spiralis.
|
pubmed:affiliation |
Department of Parasitology, College of Veterinary Medicine, University of Georgia, Athens 30602.
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|