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Clinical and Diagnostic Laboratory Immunology, 05 1996, 355-357, Vol 3, No. 3
D Harning, J Spenter, A Metsis, J Vuust and E Petersen
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.
Copyright © 1996 by the American Society for Microbiology. All rights reserved.
Recombinant Toxoplasma gondii surface antigen 1 (P30) expressed in Escherichia coli is recognized by human Toxoplasma-specific immunoglobulin M (IgM) and IgG antibodies
Laboratory of Molecular Biology, Statens Seruminstitut, Copenhagen, Denmark.
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