Open AccessHigh-resolution asymmetric structure of a Fab–virus complex reveals overlap with the receptor binding site
Author(s) -
Daniel J. Goetschius,
Samantha R. Hartmann,
Lindsey J. Organtini,
Heather Callaway,
Kai Huang,
Carol M. Bator,
Robert E. Ashley,
Alexander M. Makhov,
James F. Conway,
Colin R. Parrish,
Susan Hafenstein
Publication year - 2021
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.2025452118
Subject(s) - capsid , canine parvovirus , biology , binding site , icosahedral symmetry , immunoglobulin fab fragments , epitope , virology , minute virus of mice , virus , parvovirus , chemistry , antibody , biophysics , crystallography , complementarity determining region , parvoviridae , genetics , immunoglobulin light chain
Significance Our study makes significant progress understanding asymmetry in icosahedral viruses that would be otherwise masked by forcing homogeneity through icosahedral averaging. Using an asymmetric approach revealed the atomic-resolution structure of a complex between canine parvovirus and a strain-specific neutralizing antibody. Since species jumping is a rare event in DNA viruses, the emergence of an antibody that binds more avidly to the canine-adapted virus (and not ancestral feline equivalent) is of special interest. The Fab-bound and -unbound epitopes were solved on the same virus capsid with an atomic-resolution asymmetric map. Fab 14 stabilizes a capsid loop within the same binding site used by the receptor, suggesting capsid conformational change or steric competition with the receptor contributes to the mechanism of antibody neutralization.