ABSTRACT
Immunoglobulin (Ig) is a protein that binds to molecular determinants on pathogenic microbes, infected cells, and dysregulated self. It serves as the recognition element of the B-cell receptor (BCR) and as secreted antibody, one of the key effectors of immunity. Each antibody or BCR molecule is a homodimer of heterodimers. Each heterodimer is made up of one heavy chain and one light chain. The earliest peripheral B-cell response to novel antigen exposure is typically observed in 4-5 days, when short-lived plasmacytes can differentiate and exit the lymph node. The most common feature of the known broadly neutralizing antibodies (BNAbs) is their extraordinarily high mutation frequency. The most common feature of the known BNAbs is their extraordinarily high mutation frequency. In cases where the complete method is impractical, pairwise clonal kinship is computed. This eliminates the need to compute maximum-likelihood phylogenetic trees and provides the opportunity to relax some of the unrealistic assumptions about somatic hypermutation.
