Abstract:
:The role of binding kinetics in determining neutralizing potency for antiviral antibodies is poorly understood. While it is believed that increased steady-state affinity correlates positively with increased virus-neutralizing activity, the relationship between association or dissociation rate and neutralization potency is unclear. We investigated the effect of naturally-occurring antibody resistance mutations in the RSV F protein on the kinetics of binding to palivizumab. Escape from palivizumab-mediated neutralization of RSV occurred with reduced association rate (Kon) for binding to RSV F protein, while alteration of dissociation rate (Koff) did not significantly affect neutralizing activity. Interestingly, linkage of reduced Kon with reduced potency mirrored the effect of increased Kon found in a high-affinity enhanced potency palivizumab variant (motavizumab). These data suggest that association rate is the dominant factor driving neutralization potency for antibodies to RSV F protein antigenic site A and determines the potency of antibody somatic variants or efficiency of escape of viral glycoprotein variants.
journal_name
Virologyjournal_title
Virologyauthors
Bates JT,Keefer CJ,Slaughter JC,Kulp DW,Schief WR,Crowe JE Jrdoi
10.1016/j.virol.2014.02.010subject
Has Abstractpub_date
2014-04-01 00:00:00pages
139-44eissn
0042-6822issn
1096-0341pii
S0042-6822(14)00054-3journal_volume
454-455pub_type
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