Journal
JOURNAL OF EXPERIMENTAL MEDICINE
Volume 203, Issue 6, Pages 1567-1578Publisher
ROCKEFELLER UNIV PRESS
DOI: 10.1084/jem.20052217
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Funding
- FIC NIH HHS [TW02130, F06 TW002130] Funding Source: Medline
- NIAID NIH HHS [AI48115, R01 AI047322, AI07051, AI42732, R56 AI048115, R01 AI048115, T32 AI007051] Funding Source: Medline
- NICHD NIH HHS [HD043327, K08 HD043327] Funding Source: Medline
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Tyrosine and glycine constitute 40% of complementarity determining region 3 of the immunoglobulin heavy chain ( CDR-H3), the center of the classic antigen-binding site. To assess the role of D-H RF1-encoded tyrosine and glycine in regulating CDR-H3 content and potentially influencing B cell function, we created mice limited to a single D-H encoding asparagine, histidine, and arginines in RF1. Tyrosine and glycine content in CDR-H3 was halved. Bone marrow and spleen mature B cell and peritoneal cavity B-1 cell numbers were also halved, whereas marginal zone B cell numbers increased. Serum immunoglobulin G subclass levels and antibody titers to T-dependent and T-independent antigens all declined. Thus, violation of the conserved preference for tyrosine and glycine in D-H RF1 alters CDR-H3 content and impairs B cell development and antibody production.
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