Abstract
Glycoproteins gD-1 and gD-2 of herpes simplex virus types 1 and 2, respectively, were purified on an immunoadsorbent consisting of the type-common monoclonal antibody HD-1 linked to Sepharose. Each glycoprotein was of sufficient purity, quantity, and biological activity to be used for immunological and biochemical studies. Each glycoprotein induced high titers of type-common monospecific neutralizing antibody in mice. Amino aicd analysis indicated that gD-1 and gD-2 had similar though not identical amino acid compositions.
Full text
PDF![1099](https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f36d/256850/3507bc4536cb/jvirol00162-0365.png)
![1100](https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f36d/256850/ab1553fbc659/jvirol00162-0366.png)
![1101](https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f36d/256850/d26c6e686a2f/jvirol00162-0367.png)
![1102](https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f36d/256850/68b4ecfc9cda/jvirol00162-0368.png)
![1103](https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f36d/256850/1d2081eec57e/jvirol00162-0369.png)
![1104](https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f36d/256850/fdf17e5ae00d/jvirol00162-0370.png)
Images in this article
Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- Brown W. R., Barclay A. N., Sunderland C. A., Williams A. F. Identification of a glycophorin-like molecule at the cell surface of rat thymocytes. Nature. 1981 Feb 5;289(5797):456–460. doi: 10.1038/289456a0. [DOI] [PubMed] [Google Scholar]
- Cassai E. N., Sarmiento M., Spear P. G. Comparison of the virion proteins specified by herpes simplex virus types 1 and 2. J Virol. 1975 Nov;16(5):1327–1331. doi: 10.1128/jvi.16.5.1327-1331.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Cohen G. H., Katze M., Hydrean-Stern C., Eisenberg R. J. Type-common CP-1 antigen of herpes simplex virus is associated with a 59,000-molecular-weight envelope glycoprotein. J Virol. 1978 Jul;27(1):172–181. doi: 10.1128/jvi.27.1.172-181.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Cohen G. H., Long D., Eisenberg R. J. Synthesis and processing of glycoproteins gD and gC of herpes simplex virus type 1. J Virol. 1980 Nov;36(2):429–439. doi: 10.1128/jvi.36.2.429-439.1980. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Cohen G. H., Ponce de Leon M., Nichols C. Isolation of a herpes simplex virus-specific antigenic fraction which stimulates the production of neutralizing antibody. J Virol. 1972 Nov;10(5):1021–1030. doi: 10.1128/jvi.10.5.1021-1030.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Dulley J. R., Grieve P. A. A simple technique for eliminating interference by detergents in the Lowry method of protein determination. Anal Biochem. 1975 Mar;64(1):136–141. doi: 10.1016/0003-2697(75)90415-7. [DOI] [PubMed] [Google Scholar]
- Eisenberg R. J., Hydrean-Stern C., Cohen G. H. Structural analysis of precursor and product forms of type-common envelope glycoprotein D (CP-1 antigen) of herpes simplex virus type 1. J Virol. 1979 Sep;31(3):608–620. doi: 10.1128/jvi.31.3.608-620.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Eisenberg R. J., Ponce de Leon M., Cohen G. H. Comparative structural analysis of glycoprotein gD of herpes simplex virus types 1 and 2. J Virol. 1980 Aug;35(2):428–435. doi: 10.1128/jvi.35.2.428-435.1980. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Gibson W. Polyoma virus proteins: a description of the structural proteins of the virion based on polyacrylamide gel electrophoresis and peptide analysis. Virology. 1974 Dec;62(2):319–336. doi: 10.1016/0042-6822(74)90395-x. [DOI] [PubMed] [Google Scholar]
- Guidotti G. Membrane proteins. Annu Rev Biochem. 1972;41:731–752. doi: 10.1146/annurev.bi.41.070172.003503. [DOI] [PubMed] [Google Scholar]
- Hatefi Y., Hanstein W. G. Solubilization of particulate proteins and nonelectrolytes by chaotropic agents. Proc Natl Acad Sci U S A. 1969 Apr;62(4):1129–1136. doi: 10.1073/pnas.62.4.1129. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Kessler S. W. Rapid isolation of antigens from cells with a staphylococcal protein A-antibody adsorbent: parameters of the interaction of antibody-antigen complexes with protein A. J Immunol. 1975 Dec;115(6):1617–1624. [PubMed] [Google Scholar]
- LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
- Montgomery P. C., Dorrington K. J., Rockey J. H. Equine antihapten antibody. The molecular weights of the subunits of equine immunoglobulins. Biochemistry. 1969 Mar;8(3):1247–1258. doi: 10.1021/bi00831a060. [DOI] [PubMed] [Google Scholar]
- Pereira L., Klassen T., Baringer J. R. Type-common and type-specific monoclonal antibody to herpes simplex virus type 1. Infect Immun. 1980 Aug;29(2):724–732. doi: 10.1128/iai.29.2.724-732.1980. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Pizer L. I., Cohen G. H., Eisenberg R. J. Effect of tunicamycin on herpes simplex virus glycoproteins and infectious virus production. J Virol. 1980 Apr;34(1):142–153. doi: 10.1128/jvi.34.1.142-153.1980. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Ponce de Leon M., Hessle H., Cohen G. H. Separation of Herpes simplex virus-induced antigens by Concanavalin A affinity chromatography. J Virol. 1973 Oct;12(4):766–774. doi: 10.1128/jvi.12.4.766-774.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Spear P. G. Membrane proteins specified by herpes simplex viruses. I. Identification of four glycoprotein precursors and their products in type 1-infected cells. J Virol. 1976 Mar;17(3):991–1008. doi: 10.1128/jvi.17.3.991-1008.1976. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Vogt V. M., Eisenman R., Diggelmann H. Generation of avian myeloblastosis virus structural proteins by proteolytic cleavage of a precursor polypeptide. J Mol Biol. 1975 Aug 15;96(3):471–493. doi: 10.1016/0022-2836(75)90174-6. [DOI] [PubMed] [Google Scholar]