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Journal of Biochemistry 2006 139(3):399-406; doi:10.1093/jb/mvj042
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© 2006 The Japanese Biochemical Society.

Regular Paper

Identification and Characterization of a Neutralizing Monoclonal Antibody for the Epitope on HM-1 Killer Toxin

Dakshnamurthy Selvakumar1, Qing-Zhu Zhang1, Masahiko Miyamoto1, Yasuhiro Furuichi2 and Tadazumi Komiyama1,*

1 Department of Biochemistry, Faculty of Pharmaceutical Sciences, Niigata University of Pharmacy and Applied Life Sciences, 5-13-2 Kamishinei-cho, Niigata 950-208; and 2 GeneCare Research Institute Co. Ltd., 200 Kajiwara, Kamakura 247-0063

* To whom all correspondence should be addressed. Tel: +81-25-268-1223, Fax: +81-25-268-1230, E-mail: tkomiyam{at}niigata-pharm.ac.jp

Killer toxin-neutralizing monoclonal antibody (nmAb-KT) against HM-1 killer toxin (HM-1) produced by yeast Williopsis saturnus var. mrakii IFO 0895 reduces both the killing and glucan synthase inhibitory activity of HM-1. nmAb-KT is classified as IgG1({kappa}) and has been shown to be ineffective against HYI killer toxin produced by the related yeast W. saturnus var. saturnus IFO 0117. To determine the epitope for nmAb-KT, overlapping peptides were synthesized from the primary structure of HM-1. nmAb-KT reacted with peptides P5 (33NVHWMVTGGST43), P6 (39TGGSTDGKQG48) and P7 (44DGKQGCATIWEGS56), which represent the middle region of the HM-1 sequence. P6 reacted most strongly with nmAb-KT. Combined analysis by immunoblotting, surface plasmon resonance (SPR) analysis and yeast growth inhibition assay showed that nmAb-KT recognizes a specific epitope within peptide P6. The Kd value of nmAb-KT against HM-1 and P6 were determined to be 5.48 x 10–9 M and 1.47 x 10–6 M by SPR analysis, respectively. These results strongly indicate that nmAb-KT binds to HM-1 at the sequence 41GSTDGK46, and not to HYI at the same position. The potential active site of HM-1 involved in the killing activity against sensitive yeast is discussed.


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