Affiliation:
1. Laboratory of Molecular Biology, Statens Seruminstitut, Copenhagen, Denmark.
Abstract
The immunodominant surface antigen of Toxoplasma gondii, surface antigen 1 (SAG1), was expressed in Escherichia coli as a fusion protein containing a majority of the SAG1 protein supplied with six histidyl residues in the N-terminal end. The recombinant protein was purified on a Ni-chelate column and then on a fast-performance liquid chromatography column and was in a nonreduced condition. It was recognized by T. gondii-specific human immunoglobulin G (IgG) and IgM antibodies as well as by a mouse monoclonal antibody (S13) recognizing only nonreduced native SAG1. Antibodies induced in mice by the recombinant SAG1 recognized native SAG1 from the T. gondii RH isolate in culture. Recombinant SAG1 is suitable for use in diagnostic systems for detecting anti-SAG1-specific IgG and IgM antibodies.
Publisher
American Society for Microbiology
Subject
Microbiology (medical),Clinical Biochemistry,Immunology,Immunology and Allergy
Reference17 articles.
1. Building bridges: disulphide bond formation in the cell;Bardwell J. C. A.;Mol. Microbiol.,1994
2. Molecular analysis of the gene encoding the major surface antigen of Toxoplasma gondii;Burg J. L.;J. Immunol.,1988
3. Genetic approach to facilitate purification of recombinant proteins with a novel metal chelate adsorbent;Hochuli E.;Bio/Technology,1988
4. New metal chelate adsorbent selective for proteins and peptides containing neighbouring histidine residues;Hochuli E.;J. Chromatogr.,1987
5. Conformationally appropriate expression of the Toxoplasma antigen SAG1 (p30) in CHO cells;Kim K.;Infect. Immun.,1994
Cited by
70 articles.
订阅此论文施引文献
订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献