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Forced usage of positively charged amino acids in immunoglobulin CDR-H3 impairs B cell development and antibody production.


ABSTRACT: 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.

SUBMITTER: Ippolito GC 

PROVIDER: S-EPMC3212734 | biostudies-literature | 2006 Jun

REPOSITORIES: biostudies-literature

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Forced usage of positively charged amino acids in immunoglobulin CDR-H3 impairs B cell development and antibody production.

Ippolito Gregory C GC   Schelonka Robert L RL   Zemlin Michael M   Ivanov Ivaylo I II   Kobayashi Ryoki R   Zemlin Cosima C   Gartland G Larry GL   Nitschke Lars L   Pelkonen Jukka J   Fujihashi Kohtaro K   Rajewsky Klaus K   Schroeder Harry W HW  

The Journal of experimental medicine 20060605 6


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  ...[more]

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