Abstract
experiments showed that mAb 2A10G6 protected sucking mice from lethal dengue 1-4 viruses challenge in a dosedependent manner. Thus, we have established a novel flavivirus cross-reactive neutralizing mAb 2A10G6. Phagedisplayed random peptide library mapped the epitope of mAb 2A10G6 to a common antigenic site within the highly conserved N-terminal fusion loop peptide of flavivirus envelope protein. Functional assays confirmed that mAb 2A10G6 bind with the fusion peptide and blocks infection primarily at a step after viral attachment. Conclusion: Together, these experiments define the characteristics of a novel flavivirus cross-reactive neutralizing MAb 2A10G6 and make it a suitable candidate for humanization into a therapeutic antibody to treat severe flavivirus infections in human.
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