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pubmed-article:6863921pubmed:abstractTextPhosphorylcholine (PC), a molecule found in the cell wall of most serotypes of pneumococcus, has been used extensively as a probe for the study of network interactions during immune responses. The frequency of B lymphocytes capable of interacting with PC has not been directly examined. We used immunofluorescence to study the binding of PC and monoclonal anti-TEPC15 anti-idiotopic antibodies to murine lymphocytes. In addition to identifying PC-specific Ig molecules, PC was bound by a non-Ig molecule on the surface of a relatively large subset of B cells; this non-Ig marker shared an idiotypic determinant with the PC-binding myeloma protein HOPC8 (H8). PC-bearing R36a pneumococci bind to a similar subset of lymphocytes. This binding is inhibited specifically by PC coupled to bovine serum albumin and also by a monoclonal anti-H8 antibody. We suggest that bacterial interaction with B cells through non-Ig molecules capable of binding a dominant antigen like PC may possess functional significance, possibly during the events that lead to antibody induction by these microorganisms.lld:pubmed
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pubmed-article:6863921pubmed:dateRevised2007-11-14lld:pubmed
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pubmed-article:6863921pubmed:articleTitleBinding of phosphorylcholine by non-immunoglobulin molecules on mouse B cells.lld:pubmed
pubmed-article:6863921pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:6863921pubmed:publicationTypeResearch Support, U.S. Gov't, P.H.S.lld:pubmed
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