Abstract
Three hybridomas, designated C2, V17, and B2, were produced from BALB/c mice after immunization with measles virus. All three were directed against the virus hemagglutinin (HA). The HA is a structural peptide of the virus and constitutes a major target for the host immune response during measles infection. The monoclonal anti-HA antibodies have biological functions such as (i) measles virus neutralization in vitro, (ii) binding to acutely and persistently infected cells, and (iii) inhibition of HA-mediated Rhesus monkey erythrocyte agglutination. Different idiotypes, designated HAMM-1, HAMM-2, and HAMM-3, were defined on C2, V17, and B2, respectively, by syngeneic anti-idiotype sera against those three monoclonal antibodies. A limited cross-reactivity with the HAMM-1 idiotype was detected in sera from some BALB/c mice immunized with measles virus. The anti-idiotype sera could significantly inhibit the biological functions of the HAMM-1 and HAMM-3 idiotypes bearing monoclonal anti-HA-antibodies. This suggests a possible role for auto-anti-idiotypes in the immune response after infection with measles virus.
Full text
PDF![200](https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6819/350843/ab9f264fd6ba/iai00156-0210.png)
![201](https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6819/350843/ec665fae5e0c/iai00156-0211.png)
![202](https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6819/350843/39783df5be87/iai00156-0212.png)
![203](https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6819/350843/a1a678f255c1/iai00156-0213.png)
![204](https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6819/350843/93b430667e8b/iai00156-0214.png)
![205](https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6819/350843/0c34aceff078/iai00156-0215.png)
![206](https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6819/350843/10e89a19d7b0/iai00156-0216.png)
![207](https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6819/350843/52200c451036/iai00156-0217.png)
Images in this article
Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- Awdeh Z. L., Williamson A. R., Askonas B. A. One cell-one immunoglobulin. Origin of limited heterogeneity of myeloma proteins. Biochem J. 1970 Jan;116(2):241–248. doi: 10.1042/bj1160241. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Axén R., Porath J., Ernback S. Chemical coupling of peptides and proteins to polysaccharides by means of cyanogen halides. Nature. 1967 Jun 24;214(5095):1302–1304. doi: 10.1038/2141302a0. [DOI] [PubMed] [Google Scholar]
- Bellini W. J., McFarlin D. E., Silver G. D., Mingioli E. S., McFarland H. F. Immune reactivity of the purified hemagglutinin of measles virus. Infect Immun. 1981 Jun;32(3):1051–1057. doi: 10.1128/iai.32.3.1051-1057.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Bellini W. J., Trudgett A., McFarlin D. E. Purification of measles virus with preservation of infectivity and antigenicity. J Gen Virol. 1979 Jun;43(3):633–639. doi: 10.1099/0022-1317-43-3-633. [DOI] [PubMed] [Google Scholar]
- Bona C., Hooghe R., Cazenave P. A., Leguérn C., Paul W. E. Cellular basis of regulation of expression of idiotype. II. Immunity to anti-MOPC-460 idiotype antibodies increases the level of anti-trinitrophenyl antibodies bearing 460 idiotypes. J Exp Med. 1979 Apr 1;149(4):815–823. doi: 10.1084/jem.149.4.815. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Brient B. W., Nisonoff A. Quantitative investigations of idiotypic antibodies. IV. Inhibition by specific haptens of the reaction of anti-hapten antibody with its anti-idiotypic antibody. J Exp Med. 1970 Nov;132(5):951–962. doi: 10.1084/jem.132.5.951. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Ebers G. C., Zabriskie J. B., Kunkel H. G. Oligoclonal immunoglobulins in subacute sclerosing panencephalitis and multiple sclerosis: a study of idiotypic determinants. Clin Exp Immunol. 1979 Jan;35(1):67–75. [PMC free article] [PubMed] [Google Scholar]
- Goding J. W. The chromic chloride method of coupling antigens to erythrocytes: definition of some important parameters. J Immunol Methods. 1976;10(1):61–66. doi: 10.1016/0022-1759(76)90007-7. [DOI] [PubMed] [Google Scholar]
- Golub E. S. Idiotypes and the network hypothesis. Cell. 1980 Dec;22(3):641–642. doi: 10.1016/0092-8674(80)90536-x. [DOI] [PubMed] [Google Scholar]
- HUNTER W. M., GREENWOOD F. C. Preparation of iodine-131 labelled human growth hormone of high specific activity. Nature. 1962 May 5;194:495–496. doi: 10.1038/194495a0. [DOI] [PubMed] [Google Scholar]
- Hall W. W., Lamb R. A., Choppin P. W. Measles and subacute sclerosing panencephalitis virus proteins: lack of antibodies to the M protein in patients with subacute sclerosing panencephalitis. Proc Natl Acad Sci U S A. 1979 Apr;76(4):2047–2051. doi: 10.1073/pnas.76.4.2047. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Herzenberg L. A., Black S. J., Herzenberg L. A. Regulatory circuits and antibody responses. Eur J Immunol. 1980 Jan;10(1):1–11. doi: 10.1002/eji.1830100102. [DOI] [PubMed] [Google Scholar]
- Jerne N. K. Towards a network theory of the immune system. Ann Immunol (Paris) 1974 Jan;125C(1-2):373–389. [PubMed] [Google Scholar]
- Köhler G., Shulman M. J. Cellular and molecular restrictions of the lymphocyte fusion. Curr Top Microbiol Immunol. 1978;81:143–148. doi: 10.1007/978-3-642-67448-8_22. [DOI] [PubMed] [Google Scholar]
- Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
- Lamoyi E., Estess P., Capra J. D., Nisonoff A. Heterogeneity of an intrastrain cross-reactive idiotype associated with anti-p-azophenylarsonate antibodies of A/J mice. J Immunol. 1980 Jun;124(6):2834–2840. [PubMed] [Google Scholar]
- McFarland H. F., McFarlin D. E. Cellular immune response to measles, mumps, and vaccinia viruses in multiple sclerosis. Ann Neurol. 1979 Aug;6(2):101–106. doi: 10.1002/ana.410060204. [DOI] [PubMed] [Google Scholar]
- McFarlin D. E., Bellini W. J., Mingioli E. S., Behar T. N., Trudgett A. Monospecific antibody to the haemagglutinin of measles virus. J Gen Virol. 1980 Jun;48(Pt 2):425–429. doi: 10.1099/0022-1317-48-2-425. [DOI] [PubMed] [Google Scholar]
- Mingioli E. S., Strober W., Tourtellotte W. W., Whitaker J. N., McFarlin D. E. Quantitation of IgG, IgA and IgM in the CSF by radioimmunoassay. Neurology. 1978 Oct;28(10):991–995. doi: 10.1212/wnl.28.10.991. [DOI] [PubMed] [Google Scholar]
- Mountcastle W. E., Choppin P. W. A comparison of the polypeptides of four measles virus strains. Virology. 1977 May 15;78(2):463–474. doi: 10.1016/0042-6822(77)90123-4. [DOI] [PubMed] [Google Scholar]
- Noppe M., Lowenthal A., Karcher D., Gheuens J. A two-site immunoradiometric assay for the determination of alpha-albumin. J Immunol Methods. 1979 May 10;27(1):75–81. doi: 10.1016/0022-1759(79)90240-0. [DOI] [PubMed] [Google Scholar]
- Norrby E., Gollmar Y. Identification of measles virus-specific hemolysis-inihibiting antibodies separate from hemagglutination-inhibiting antibodies. Infect Immun. 1975 Feb;11(2):231–239. doi: 10.1128/iai.11.2.231-239.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Norrby E., Hammarskjöld B. Structural components of measles virus. Microbios. 1972 Jan;5(17):17–29. [PubMed] [Google Scholar]
- OUCHTERLONY O. Diffusion-in-gel methods for immunological analysis. Prog Allergy. 1958;5:1–78. [PubMed] [Google Scholar]
- Sher A., Cohn M. Effect of haptens on the reaction of anti-idiotype antibody with a mouse anti-phosphorylcholine plasmacytoma protein. J Immunol. 1972 Jul;109(1):176–178. [PubMed] [Google Scholar]
- Trudgett A., Bellini W. J., Mingioli E. S., McFarlin D. E. Antibodies to the structural polypeptides of measles virus following acute infection and in SSPE. Clin Exp Immunol. 1980 Mar;39(3):652–656. [PMC free article] [PubMed] [Google Scholar]
- Wechsler S. L., Weiner H. L., Fields B. N. Immune response in subacute sclerosing panencephalitis: reduced antibody response to the matrix protein of measles virus. J Immunol. 1979 Aug;123(2):884–889. [PubMed] [Google Scholar]
- Weigert M., Raschke W. C., Carson D., Cohn M. Immunochemical analysis of the idiotypes of mouse myeloma proteins with specificity for levan or dextran. J Exp Med. 1974 Jan 1;139(1):137–147. doi: 10.1084/jem.139.1.137. [DOI] [PMC free article] [PubMed] [Google Scholar]