10/6/2023 0 Comments Aive antibody repertoireThere are many genes for each of the V, D, and J segments, which can be matched up in different combinations to produce a diverse range of antibody sequences. The heavy chain is encoded from variable, joining, and diversity (D) segments. The sequence for the light-chain variable region (Fv) is made up of two segments: the variable segment (V) and the joining segment (J). Each of these is encoded by multiple gene segments that are spliced together using a process called V(D)J recombination ( 7). Antibodies are composed of two types of protein chain, known as the heavy and light chains ( Fig. This diversity is a result of how the proteins are encoded in the genome. It is estimated that the human antibody repertoire contains around 10 13 unique sequences ( 6). Antibodies are currently the largest class of biotherapeutic ( 5). This property has made antibodies highly successful as therapeutics to date, 87 have been approved for use in the clinic across a number of disease areas, and many more are undergoing clinical trials ( 3, 4). The ability of the immune system to respond to a huge range of antigens originates in the diversity of the antibodies that can be generated-antibodies can be produced that bind to nearly every antigen, with both high specificity and affinity ( 2). They are able to neutralize and initiate the removal of foreign entities (known as antigens) from the body by binding to them ( 1). They are produced by B cells and are either secreted or membrane-bound (in the latter case, they are known as B-cell receptors, or BCRs). We also consider how structural information can be used to enhance these data and may lead to more accurate depictions of the sequence space and to applications in the discovery of new therapeutics.Īntibodies are proteins that play a key role in the adaptive immune response. We highlight its utility for providing insights into how the naive immune repertoire is generated and how it responds to antigens. In this review, we discuss the many ways in which BCR repertoire data have been or could be exploited. This wealth of data has created opportunities to learn more about our immune system. antigen-inexperienced) and that after immunization. Repertoires are available that represent both the naive state ( i.e. The Observed Antibody Space database, for example, currently contains over a billion sequences from 68 different studies. Next-generation sequencing technologies are being increasingly used to query the antibody, or B-cell receptor (BCR), sequence repertoire, and the amount of BCR data in public repositories is growing. The antibodies present in an organism therefore report on its immune status, describe its innate ability to deal with harmful substances, and reveal how it has previously responded. In an organism, after antigen exposure, antibodies specific to that antigen are enriched through clonal selection, expansion, and somatic hypermutation. ![]() Because they can be developed to bind to many disease agents, antibodies can be used as therapeutics. Mammals can efficiently create vast numbers of antibodies with different sequences capable of binding to any antigen with high affinity and specificity. Antibodies are vital proteins of the immune system that recognize potentially harmful molecules and initiate their removal.
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