Abstract
A monoclonal antibody, 5-5B, which neutralizes Shiga toxin 1 (Stx1) cytotoxicity of Escherichia coli, was constructed. An epitope analysis indicated that Asn55 in Stx1 B subunit was an important residue. This result and our previous results using an anti-Stx2 monoclonal antibody indicate that the region around the cysteine residue of the disulfide bond might be important for the neutralization of Stx cytotoxicity, making it a potential vaccination candidate.
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Nakao, H., Kataoka, C., Kiyokawa, N., Fujimoto, J., Yamasaki, S., & Takeda, T. (2002). Monoclonal antibody to Shiga toxin 1, which blocks receptor binding and neutralizes cytotoxicity. Microbiology and Immunology, 46(11), 777–780. https://doi.org/10.1111/j.1348-0421.2002.tb02764.x
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