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Clinical and Diagnostic Laboratory Immunology, March 2001, p. 454-459, Vol. 8, No. 2
1071-412X/01/$04.00+0   DOI: 10.1128/CDLI.8.2.454-459.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Detection of Serum Thermolabile beta -2 Macroglycoprotein (Hakata Antigen) by Enzyme-Linked Immunosorbent Assay Using Polysaccharide Produced by Aerococcus viridans

Mitsushi Tsujimura,1 Chuzo Ishida,1 Yasuko Sagara,1 Takashi Miyazaki,1 Koichi Murakami,2 Hiroshi Shiraki,1,* Kazuo Okochi,1 and Yoshiaki Maeda1

Fukuoka Red Cross Blood Center, Chikushino, Fukuoka 818-8588,1 and Pathology and Bacteriology Division, Fukuoka Institute of Health and Environmental Sciences, Dazaifu, Fukuoka 818-0135,2 Japan

Received 29 June 2000/Returned for modification 19 October 2000/Accepted 11 December 2000

Although a serum thermolabile beta -2 macroglycoprotein (TMG) may play a role in host defense as a lectin, little is known of its related physiological functions, mainly due to a lack of appropriate methods for tracing the functions of TMG. We identified a polysaccharide from Aerococcus viridans, PSA, which reacts with TMG, and based on this finding, we developed an enzyme-linked immunosorbent assay to trace the functions of TMG. Using ethanol precipitation and DEAE-Sepharose and Sephacryl S-400 column chromatographies, we isolated PSA from cultured medium of A. viridans, and it exhibited specific binding against TMG in blood samples. In sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), the isolated PSA showed ladder bands that implied the existence of repeating units composed of D-glucose, N-acetyl-D-glucosamine, D-mannose, and D-xylose, as confirmed by gas chromatography-mass spectrometry. SDS-PAGE and immunochemical analysis, using rabbit anti-TMG antibody, showed that PSA specifically binds solely to intact serum TMG but not to TMG heated at 56°C for 30 min, a condition under which antigenicity is lost. TMG in serum samples bound to PSA in a dose-dependent manner, and this binding was clearly suppressed by addition of PSA. These observations indicate that PSA is a useful adsorbent to TMG and can be used to develop appropriate methods for tracing the functions of TMG.

* Corresponding author. Mailing address: Fukuoka Red Cross Blood Center, 1-2-1 Kamikoga, Chikushino, Fukuoka 818-8588, Japan. Phone: 81-92-921-1400. Fax: 81-92-921-0799. E-mail: fbc.shiraki{at}fukuoka.emailne.jp.

Clinical and Diagnostic Laboratory Immunology, March 2001, p. 454-459, Vol. 8, No. 2
1071-412X/01/$04.00+0   DOI: 10.1128/CDLI.8.2.454-459.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


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