Open AccessRecombinant Toxoplasma gondii surface antigen 1 (P30) expressed in Escherichia coli is recognized by human Toxoplasma-specific immunoglobulin M (IgM) and IgG antibodies
Author(s) -
D Harning,
Johanne Spenter,
A. Metsis,
Jens Vuust,
Eskild Petersen
Publication year - 1996
Publication title -
clinical and diagnostic laboratory immunology
Language(s) - English
Resource type - Journals
eISSN - 1098-6588
pISSN - 1071-412X
DOI - 10.1128/cdli.3.3.355-357.1996
Subject(s) - toxoplasma gondii , recombinant dna , antibody , antigen , microbiology and biotechnology , monoclonal antibody , biology , fusion protein , escherichia coli , virology , chemistry , biochemistry , immunology , gene
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.