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作 者:Jan Novak Matthew B.Renfrow R.Glenn King Colin Reily Todd J.Green
机构地区:[1]Department of Microbiology,University of Alabama at Birmingham,Birmingham,AL,USA [2]Department of Biochemistry and Molecular Genetics,University of Alabama at Birmingham,Birmingham,AL,USA
出 处:《Cellular & Molecular Immunology》2023年第3期305-307,共3页中国免疫学杂志(英文版)
基 金:NIH grants Al149431,GM098539,DK078244,DK082753,DK106341,Al14273,and Al162236.
摘 要:Human adaptive immunity involves the production and secretion of antibodies by differentiated B cells(ie.,antibody-secreting cells,also called plasma cells)in response to antigens.These secreted antigen-specific antibodies are immunoglobulins that are present at substantial concentrations in blood,mucosal secretions,and breast milk.Structurally,human immunoglobulins consist of two identical heavy(H)chains and two identical light(L)chains that are connected by disulfide bridges to form a homodimer of heterodimers(ie.,H+Ll2).Each heterodimer consists of one H chain linked with one L chain,whereas the homodimer is formed by linking two H chains together.The genes for both the L and H chains are encoded by ligated gene segments that are genetically rearranged during V(D)J recombination,a process that endows each B cell with a unique receptor,giving rise to the enormous diversity of the B-cell antigen receptor repertoire.
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