Cookies on this website
We use cookies to ensure that we give you the best experience on our website. If you click 'Continue' we'll assume that you are happy to receive all cookies and you won't see this message again. Click 'Find out more' for information on how to change your cookie settings.

We have shown that the core antigen receptor of all five isotypes is composed of immunoglobulin in association with a common heterodimeric alpha/beta sheath. The stoichiometry of the association is unknown although preliminary evidence points to it being an IgH2L2 [alpha/beta]2 association. Studies with chimaeric molecules indicate that much of the immunoglobulin-sheath interaction must occur through the carboxyterminal end of the molecule with particular importance being given to the linker-transmembrane region. The glycosylation of the alpha chain differs according to the isotype with which it is associated. There are two sites for N-linked glycosylation on the alpha chain (Asn-30 and Asn-40); both sites are used. Mutation of Asn-30 alone decreases but does not abolish surface expression of the antigen receptor complex. Mutation of both sites prevents expression of the surface IgM[alpha/beta] complex but not of a surface IgD[alpha/beta] complex. Moreover, the pattern of alpha glycosylation is considerably affected by changes in the linker region between C mu 4 and the transmembrane, giving further support to the importance of this region in immunoglobulin-sheath interaction. Unlike IgM, IgD and IgG2b do not require alpha/beta for transport to the cell surface and can be expressed on the surface without either sheath or glycosyl phosphatidylinositol anchor. This finding may reflect that the IgD transmembrane region is significantly less hydrophobic than that of IgM; however, it should be noted that is not clear whether naked IgD exists in vivo. In fact, we have found that the alpha/beta sheath is necessary in order to facilitate efficient internalization and presentation of antigen by membrane immunoglobulin. The sheath presumably also plays a major role in potentiating transmembrane signalling. However, mutant receptors that do not associate with the alpha/beta sheath are nevertheless able to trigger phosphorylation of cellular proteins on tyrosine residues following cross-linking. Also, in addition to the alpha/beta sheath, other transmembrane proteins associate with the B-cell antigen receptor although they are not required in order to potentiate surface transport. It may be interaction with one of these other associated transmembrane proteins or, alternatively, interaction between the immunoglobulin cytoplasmic tail and, say, the cytoskeleton, that enables antigen receptors lacking the alpha/beta sheath to give rise to cellular signalling.

Original publication

DOI

10.1111/j.1600-065x.1993.tb00841.x

Type

Journal article

Journal

Immunol Rev

Publication Date

04/1993

Volume

132

Pages

147 - 161

Keywords

Amino Acid Sequence, Animals, Antigens, CD, B-Lymphocytes, CD79 Antigens, Glycosylation, Immunoglobulin Isotypes, Immunoglobulins, Membrane Glycoproteins, Membrane Proteins, Mice, Molecular Sequence Data, Receptors, Antigen, B-Cell, Receptors, Immunologic, Tumor Cells, Cultured