Letter | Published:

Receptor interactions on the membrane of resting and activated B cells

Abstract

LIPOPOLYSACCHARIDE (LPS) activates one-third of the B cells in mouse spleen, inducing proliferation and maturation to immunoglobulin secretion1. The surface structure functioning as receptor in the triggering process is specific for the lipid A moiety of LPS2, and is encoded by a gene mapped on chromosome 4 (ref. 3), for which two nonfunctional alleles are known (refs 4, 5 and A. C. and T. Meo, in preparation). We have recently described an antiserum which seemed specific for that LPS receptor (LPSR) on the basis of morphological, functional and genetic evidence6,7. The polyclonality of B cell responses to LPS8 has excluded the participation of immunoglobulin combining sites in the process of triggering. The existence of two LPS nonresponder mutants, which display normal triggering behaviour with other reagents and a normal complement of immunoglobulin positive cells5,9, also suggested that LPS activation proceeds independently of surface immunoglobulin receptors. The finding of the inhibition of LPS activation by anti-immunoglobulin antibodies, however, suggested that mitogen receptors and surface immunoglobulins could be interacting on the B-cell membrane10. We report here direct morphological evidence that supports the existence of such interactions.

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