Abstract
In 1981, Auffray et al. [Auffray, C., Sikorav, J. L., Ollo, R. & Rougeon, F. (1981) Ann. Immunol. (Inst. Pasteur) 132D, 77-88] reported a partial cDNA sequence of the heavy chain from the ABPC48 plasmacytoma whose protein product had previously been shown to bind bacterial and grass levan. In the cDNA sequence the second half-cystine of the heretofore invariant disulfide bridge had been replaced by a tyrosine. Since the presence of invariant variable-region disulfide bridges has been considered a basic structural feature of the antibody molecule necessary for proper folding and function, we have analyzed the heavy chain protein produced by ABPC48. Our results indicate that heavy chains from ABPC48 quantitatively express tyrosine in place of the normally occurring second half-cystine in the variable region. Furthermore, this antibody population is capable of both binding antigen and subsequent precipitation. Thus, the presence of a disulfide bridge in the heavy-chain variable region does not appear necessary for proper function of this antibody and may not be obligatory for antibody function in general, as has been assumed previously.
Full text
PDF
Images in this article
Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- Cisar J., Kabat E. A., Liao J., Potter M. Immunochemical studies on mouse myeloma proteins reactive with dextrans or with fructosans and on human antilevans. J Exp Med. 1974 Jan 1;139(1):159–179. doi: 10.1084/jem.139.1.159. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Das M. K., Glaudemans C. P. A general chromatographic procedure for the purification of murine myeloma immunoglobulins A. Carbohydr Res. 1978 Apr;62(1):165–168. doi: 10.1016/s0008-6215(00)83388-1. [DOI] [PubMed] [Google Scholar]
- Davies D. R., Metzger H. Structural basis of antibody function. Annu Rev Immunol. 1983;1:87–117. doi: 10.1146/annurev.iy.01.040183.000511. [DOI] [PubMed] [Google Scholar]
- Jolley M. E., Glaudemans C. P., Rudikoff S., Potter M. Structural requirements for the binding of derivatives of D-galactose to two homogeneous murine immunoglobulins. Biochemistry. 1974 Jul 16;13(15):3179–3184. doi: 10.1021/bi00712a028. [DOI] [PubMed] [Google Scholar]
- Padlan E. A. Structural basis for the specificity of antibody-antigen reactions and structural mechanisms for the diversification of antigen-binding specificities. Q Rev Biophys. 1977 Feb;10(1):35–65. doi: 10.1017/s0033583500000135. [DOI] [PubMed] [Google Scholar]
- Poljak R. J., Amzel L. M., Avey H. P., Chen B. L., Phizackerley R. P., Saul F. Three-dimensional structure of the Fab' fragment of a human immunoglobulin at 2,8-A resolution. Proc Natl Acad Sci U S A. 1973 Dec;70(12):3305–3310. doi: 10.1073/pnas.70.12.3305. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Potter M. Antigen-binding myeloma proteins of mice. Adv Immunol. 1977;25:141–211. [PubMed] [Google Scholar]
- Rudikoff S., Pawlita M., Pumphrey J., Mushinski E., Potter M. Galactan-binding antibodies. Diversity and structure of idiotypes. J Exp Med. 1983 Nov 1;158(5):1385–1400. doi: 10.1084/jem.158.5.1385. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Segal D. M., Padlan E. A., Cohen G. H., Rudikoff S., Potter M., Davies D. R. The three-dimensional structure of a phosphorylcholine-binding mouse immunoglobulin Fab and the nature of the antigen binding site. Proc Natl Acad Sci U S A. 1974 Nov;71(11):4298–4302. doi: 10.1073/pnas.71.11.4298. [DOI] [PMC free article] [PubMed] [Google Scholar]