![]() Springer Semin Immunopathol 26(4):385–404īinder CJ, Horkko S, Dewan A, Chang MK, Kieu EP, Goodyear CS et al (2003) Pneumococcal vaccination decreases atherosclerotic lesion formation: molecular mimicry between Streptococcus pneumoniae and oxidized LDL. Proc Natl Acad Sci U S A 109(48):19745–19750īinder CJ, Silverman GJ (2005) Natural antibodies and the autoimmunity of atherosclerosis. Grönwall C, Chen Y, Vas J, Khanna S, Thiel S, Corr M et al (2012) MAPK phosphatase-1 is required for regulatory natural autoantibody-mediated inhibition of TLR responses. Shaw PX, Goodyear CS, Chang MK, Witztum JL, Silverman GJ (2003) The autoreactivity of anti-phosphorylcholine antibodies for atherosclerosis-associated neo-antigens and apoptotic cells. Shaw PX, Horkko S, Chang MK, Curtiss LK, Palinski W, Silverman GJ et al (2000) Natural antibodies with the T15 idiotype may act in atherosclerosis, apoptotic clearance, and protective immunity. J Immunol 183(2):1346–1359Ĭhen Y, Park YB, Patel E, Silverman GJ (2009) IgM antibodies to apoptosis-associated determinants recruit C1q and enhance dendritic cell phagocytosis of apoptotic cells. Curr Top Microbiol Immunol 252:211–220Ĭhen Y, Khanna S, Goodyear CS, Park YB, Raz E, Thiel S et al (2009) Regulation of dendritic cells and macrophages by an anti-apoptotic cell natural antibody that suppresses TLR responses and inhibits inflammatory arthritis. J Immunol 133(6):3308–3312īos NA, Cebra JJ, Kroese FG (2000) B-1 cells and the intestinal microflora. McDaniel LS, Benjamin WH Jr, Forman C, Briles DE (1984) Blood clearance by anti-phosphocholine antibodies as a mechanism of protection in experimental pneumococcal bacteremia. Lutz HU, Binder CJ, Kaveri S (2009) Naturally occurring auto-antibodies in homeostasis and disease. Yang Y, Wang C, Yang Q, Kantor AB, Chu H, Ghosn EE et al (2015) Distinct mechanisms define murine B cell lineage immunoglobulin heavy chain (IgH) repertoires. Herzenberg LA, Herzenberg LA (1989) Toward a layered immune system. Lavinder JJ, Horton AP, Georgiou G, Ippolito GC (2015) Next-generation sequencing and protein mass spectrometry for the comprehensive analysis of human cellular and serum antibody repertoires. These methods will be used to investigate the effects of microbial virulence factors on host defenses, during autoimmune responses, and in B-cell malignancies. By these methods we have begun to define the molecular differences in the IgA1 and IgA2 responses occurring simultaneously in different donors. For exploration of human IgA responses, we have designed a duplexing antisense constant region primer that efficiently amplifies, side-by-side, heavy chain transcripts of both the IgA1 and IgA2 subclasses. To avoid biases potentially introduced by upstream oligonucleotide primers that hybridize to variable region framework regions, our approach also uses rapid amplification of cDNA ends (RACE) of antibody transcripts. To recover representative repertoire libraries, we make our libraries from antibody gene transcript templates (i.e., cDNA), as these are closer reflections of the immune repertoire expressed at the antibody protein level. In these studies we can characterize the IgA clonal diversity of B-cell populations obtained from any donor. In fact, IgA is secreted at all mucosal surfaces, and it is also secreted in the perspiration that coats our cutaneous surfaces. Here we study IgA repertoires, as more IgA antibodies are synthesized in the human body on a daily level than all other isotypes combined. For investigations of human B-cell receptor (BCR) repertoires, we have developed a protocol for large-scale surveys of human antibody heavy chain (VH) rearrangements.
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