Commonality despite exceptional diversity in the baseline human antibody repertoire
In principle, humans can produce an antibody response to any non-self-antigen molecule in the appropriate context. This flexibility is achieved by the presence of a large repertoire of naive antibodies, the diversity of which is expanded by somatic hypermutation following antigen exposure.
High frequency of shared clonotypes in human B cell receptor repertoires
The human genome contains approximately 20 thousand protein-coding genes1, but the size of the collection of antigen receptors of the adaptive immune system that is generated by the recombination of gene segments with non-templated junctional additions (on B cells) is unknown—although it is certainly orders of magnitude larger.
HereReproducibility and Reuse of Adaptive Immune Receptor Repertoire Data
High-throughput sequencing (HTS) of immunoglobulin (B-cell receptor, antibody) and T-cell receptor repertoires has increased dramatically since the technique was introduced in 2009 (1–3). This experimental approach explores the maturation of the adaptive immune system and its response to antigens, pathogens, and disease conditions in exquisite detail.
Adaptive Immune Receptor Repertoire Community recommendations for sharing immune-repertoire sequencing data
Antigen specificity is a cardinal feature of adaptive immunity that underlies immune homeostasis and control of pathogenic attack in higher vertebrates.
Mosaic deletion patterns of the human antibody heavy chain gene locus shown by Bayesian haplotyping
Analysis of antibody repertoires by high-throughput sequencing is of major importance in understanding adaptive immune responses. Our knowledge of variations in the genomic loci encoding immunoglobulin genes is incomplete, resulting in conflicting VDJ gene assignments and biased genotype and haplotype inference.