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Monoclonal Antibody to Shiga Toxin 1, Which Blocks Receptor Binding and Neutralizes Cytotoxicity
Author(s) -
Nakao Hiroshi,
Kataoka Chiwa,
Kiyokawa Nobutaka,
Fujimoto Junichiro,
Yamasaki Shinji,
Takeda Tae
Publication year - 2002
Publication title -
microbiology and immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.664
H-Index - 70
eISSN - 1348-0421
pISSN - 0385-5600
DOI - 10.1111/j.1348-0421.2002.tb02764.x
Subject(s) - cytotoxicity , monoclonal antibody , shiga toxin , biology , escherichia coli , epitope , antibody , shiga like toxin , toxin , microbiology and biotechnology , stx2 , complement dependent cytotoxicity , virology , biochemistry , antibody dependent cell mediated cytotoxicity , immunology , in vitro , gene
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.