50 Years of structural immunology
Autor: | Ian A. Wilson, Robyn L. Stanfield |
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Rok vydání: | 2021 |
Předmět: |
0301 basic medicine
Cellular immunity Protein Folding CoV coronavirus Adaptive Immunity Antibodies Viral Biochemistry hGH human growth hormone Antibody Specificity humoral immunity antibodies immune recognition Antigens Viral Toll-like receptor Antigen Presentation Crystallography TCR T cell receptor RBD receptor-binding domain Acquired immune system NA neuraminidase MR molecular replacement EPOR erythropoietin receptor TLR Toll-like receptor Antigen presentation Receptors Antigen T-Cell T cells cellular immunity Biology Major histocompatibility complex VLR variable lymphocyte receptor History 21st Century 03 medical and health sciences Immune system Antigen PDB Protein Data Bank Allergy and Immunology TLR CDR complementarity-determining region VLR Animals Humans MHC major histocompatibility complex Protein Interaction Domains and Motifs NTD N-terminal domain Receptors Cytokine Molecular Biology Innate immune system 030102 biochemistry & molecular biology SARS-CoV-2 JBC Reviews viral antigens COVID-19 Cell Biology History 20th Century Ig immunoglobulin Immunity Innate V(D)J Recombination 030104 developmental biology Immunology biology.protein RSV respiratory syncytial virus MHC microbial pathogens EPO erythropoietin GP glycoprotein NKT cell natural killer T cell HA hemagglutinin |
Zdroj: | The Journal of Biological Chemistry |
ISSN: | 1083-351X |
Popis: | Fifty years ago, the first landmark structures of antibodies heralded the dawn of structural immunology. Momentum then started to build toward understanding how antibodies could recognize the vast universe of potential antigens and how antibody-combining sites could be tailored to engage antigens with high specificity and affinity through recombination of germline genes (V, D, J) and somatic mutation. Equivalent groundbreaking structures in the cellular immune system appeared some 15 to 20 years later and illustrated how processed protein antigens in the form of peptides are presented by MHC molecules to T cell receptors. Structures of antigen receptors in the innate immune system then explained their inherent specificity for particular microbial antigens including lipids, carbohydrates, nucleic acids, small molecules, and specific proteins. These two sides of the immune system act immediately (innate) to particular microbial antigens or evolve (adaptive) to attain high specificity and affinity to a much wider range of antigens. We also include examples of other key receptors in the immune system (cytokine receptors) that regulate immunity and inflammation. Furthermore, these antigen receptors use a limited set of protein folds to accomplish their various immunological roles. The other main players are the antigens themselves. We focus on surface glycoproteins in enveloped viruses including SARS-CoV-2 that enable entry and egress into host cells and are targets for the antibody response. This review covers what we have learned over the past half century about the structural basis of the immune response to microbial pathogens and how that information can be utilized to design vaccines and therapeutics. |
Databáze: | OpenAIRE |
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