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Appl. Environ. Microbiol., 04 1997, 1214-1218, Vol 63, No. 4
Copyright © 1997, American Society for Microbiology

Epitope regions in the heavy chain of Clostridium botulinum type E neurotoxin recognized by monoclonal antibodies

T Kubota, T Watanabe, N Yokosawa, K Tsuzuki, T Indoh, K Moriishi, K Sanda, Y Maki, K Inoue and N Fujii
Department of Microbiology, Sapporo Medical University, Japan.

Seventeen monoclonal antibodies (MAbs) were previously established against the heavy chain (Hc) of botulinum type E neurotoxin in BALB/c mice immunized with the type E toxoid. Five MAbs (LE15-5, LE34-6, EK19- 7, EK21-4, and AE27-9) showed toxin-neutralizing activity in mice. Two of the five MAbs, EK19-7 and EK21-4, recognized the regions located at amino acid positions 731 to 787 and 811 to 897, respectively. One of the remaining three antibodies (LE34-6) reacted with the amino acid sequence VIKAIN, at amino acid positions 663 to 668, closed by the ion channel-forming domain. It is suggested that the ion channel-forming domain may also be associated with the blocking of acetylcholine release. Furthermore, the amino acid sequence YLTHMRD within 30 residues of the C-terminal region of the Hc component seemed to be recognized by LE15-5. It has been reported that the binding domain of the type E toxin is located on the C-terminal half of the Hc component. Therefore, the neutralizing activity of LE15-5 antibody may be attributed to its ability to block the binding of neurotoxin to the receptor of target cells.

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