bioRxivMicrobiologyPreprint
Mechanisms of antibody binding revealed by asymmetric Fab-virus complexes
D. J. Goetschius, S. R. Hartmann, L. J. Organtini, H. Callaway, K. Huang, C. M. Bator, R. E. Ashley, A. M. Makhov, J. F. Conway, C. R. Parrish, S. L. Hafenstein
Abstract
Overlap on the surface of parvovirus capsids between the antigenic epitope and the receptor binding site contributes to species jumping. Mab 14 strongly binds and neutralizes canine, but not feline parvovirus. The high resolution map of the canine parvovirus capsid complexed with Fab 14 was used to solve local structures of the Fab-bound and -unbound antigenic sites extracted from the same complex. The subsequent analysis includes a new method for using cryo EM to investigate complementarity of antibody binding.
- organism: virus
- assay: structural biology
- research focus: host-pathogen & immune response
- approach: microscopy & imaging analysis
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