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- W3110381446 abstract "Zika virus (ZIKV), a mosquito-borne human flavivirus that causes microcephaly and other neurological disorders, has been a recent focus for the development of flavivirus vaccines and therapeutics. We report here a 4.0 Å resolution structure of the mature ZIKV in complex with ADI-30056, a ZIKV-specific human monoclonal antibody (hMAb) isolated from a ZIKV infected donor with a prior dengue virus infection. The structure shows that the hMAb interactions span across the E protein dimers on the virus surface, inhibiting conformational changes required for the formation of infectious fusogenic trimers similar to the hMAb, ZIKV-117. Structure-based functional analysis, and structure and sequence comparisons, identified ZIKV residues essential for neutralization and crucial for the evolution of highly potent E protein crosslinking Abs in ZIKV. Thus, this epitope, ZIKV’s “Achilles heel”, defined by the contacts between ZIKV and ADI-30056, could be a suitable target for the design of therapeutic antibodies." @default.
- W3110381446 created "2020-12-07" @default.
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- W3110381446 date "2020-11-24" @default.
- W3110381446 modified "2023-09-25" @default.
- W3110381446 title "Structural Basis of Zika Virus Specific Neutralization in Subsequent Flavivirus Infections" @default.
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- W3110381446 doi "https://doi.org/10.3390/v12121346" @default.
- W3110381446 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/7760643" @default.
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