Data from: Antibody selection and amino acid reversions

Pathogens adapt to antibody surveillance through amino acid replacements
in targeted protein regions, or epitopes, that interfere with antibody
binding. However, such escape mutations may exact a fitness cost due to
impaired protein function. Here, it is hypothesised that the recurring
generation of specific neutralising antibodies to an epitope region as it
evolves in response to antibody selection will cause amino acid reversions
by releasing early escape mutations from immune selection. The
plausibility of this hypothesis was tested with stochastic simulation of
adaptation at the molecular sequence level in finite populations. Under
the conditions of strong selection and weak mutation, the rates of allele
fixation and amino acid reversion increased with population size and
selection coefficients. These rates decreased with population size,
however, if mutation became strong, because clonal interference reduced
the rate of adaptation. The model successfully predicts the rate of
reversion per allele fixation for an important human immunodeficiency
virus type 1 (HIV-1) antibody epitope region. Therefore, antibody
selection may generate complex adaptive dynamics.