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- W2234972189 abstract "Twenty three stable monoclonal antibodies (mAbs) against β1-bungarotoxin (β1-bgt) were prepared by the hybridoma technique. Seven of the 23 mAbs (mAbs 2, 6, 8, 11, 17, 21 and 22) could inhibit more than 70% of phospholipase A2 activity of β1-bgt and neutralize the toxin. Six of these neutralizing mAbs (mAbs 2, 6, 8, 17, 21 and 22) recognized continuous epitopes on the A chain of β1-bgt and the other one (mAb 11) recognized a conformational epitope on the toxin. The continuous epitopes of these six mAbs were mapped using synthetic peptide and proteolytic enzymes. Experimental results indicate that mAb 17 recognized the A-chain residues 31-37; mAbs 2 and 8 recognized residues 46-51; mAbs 21 and 22 recognized residues 91-98; and mAb 6 recognized residue 100-106. The competitive-antibody-binding inhibition experiments showed that the affinity of these neutralizing mAbs to the native β1-bgt is compatible with synthetic peptides. Furthermore, mice immunized with BSA-conjugated A-chain-peptide sequences A(31-37), A(46-51), A(91-98) or A(100-106) were protected from a high-dose β1-bgt challenge. Subsequently, the peptide-immunized sera were passively injected into Balb/c mice and a significantly protective effect was also observed. To our knowledge, this study is the first systematic demonstration of multiple neutralizing B-cell epitopes of β1-bgt, and this study is also the first report of the protective synthetic-peptide vaccine against β1-bgt challenge." @default.
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- W2234972189 date "1998-02-15" @default.
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- W2234972189 title "Neutralizing epitope mapping of six β1-bungarotoxin monoclonal antibodies and its application in β1-bungarotoxin peptide vaccine design" @default.
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- W2234972189 doi "https://doi.org/10.1042/bj3300497" @default.
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