Abstract
A glycoprotein with affinity for the Fc region of immunoglobulin was isolated from extracts of cultured cells infected with herpes simplex virus type 1, and experiments were done to characterize its properties and to investigate whether it could account for the Fc-binding activity previously demonstrated on the surfaces of intact herpes simplex virus-infected cells. The technique of affinity chromatography was used to identify and isolate the Fc-binding glycoprotein and to demonstrate the specificity of its interaction with immunoglobulin G-Fc. Although three electrophoretically distinguishable Fc-binding polypeptides were identified by affinity chromatography, these three species appear to be different forms of the same translation product, based on comparisons of proteolytic digestion products and on the kinetics of appearance of each form after a brief pulse with radioactive amino acids. The results suggest that one polypeptide, designated pE, is processed to yield gE1, which is in turn processed to yield gE2. Both gE1 and gE2 are glycosylated membrane proteins and both can be labeled by the lactoperoxidase-catalyzed radioiodination of intact infected cells, indicating the presence of these proteins in surface membranes of the cells. Increases in the amounts of gE1 and gE2 at the cell surface were found to parallel the increase in Fc-binding activity of intact infected cells.
Full text
PDFImages in this article
Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- Adler R., Glorioso J. C., Cossman J., Levine M. Possible role of Fc receptors on cells infected and transformed by herpesvirus: escape from immune cytolysis. Infect Immun. 1978 Aug;21(2):442–447. doi: 10.1128/iai.21.2.442-447.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Bonner W. M., Laskey R. A. A film detection method for tritium-labelled proteins and nucleic acids in polyacrylamide gels. Eur J Biochem. 1974 Jul 1;46(1):83–88. doi: 10.1111/j.1432-1033.1974.tb03599.x. [DOI] [PubMed] [Google Scholar]
- Byrt P., Ada G. L. An in vitro reaction between labelled flagellin or haemocyanin and lymphocyte-like cells from normal animals. Immunology. 1969 Oct;17(4):503–516. [PMC free article] [PubMed] [Google Scholar]
- Cassai E., Manservigi R., Corallini A., Terni M. Plaque dissociation of herpes simplex viruses: biochemical and biological characters of the viral variants. Intervirology. 1975;6(4-5):212–223. doi: 10.1159/000149476. [DOI] [PubMed] [Google Scholar]
- Cleveland D. W., Fischer S. G., Kirschner M. W., Laemmli U. K. Peptide mapping by limited proteolysis in sodium dodecyl sulfate and analysis by gel electrophoresis. J Biol Chem. 1977 Feb 10;252(3):1102–1106. [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]
- Costa J. C., Rabson A. S. Role of Fc receptors in herpes simplex virus infection. Lancet. 1975 Jan 11;1(7898):77–78. doi: 10.1016/s0140-6736(75)91077-6. [DOI] [PubMed] [Google Scholar]
- Costa J., Rabson A. S., Yee C., Tralka T. S. Immunoglobulin binding to herpes virus-induced Fc receptors inhibits virus growth. Nature. 1977 Sep 15;269(5625):251–252. doi: 10.1038/269251a0. [DOI] [PubMed] [Google Scholar]
- Costa J., Yee C., Nakamura Y., Rabson A. Characteristics of the Fc receptor induced by herpes simplex virus. Intervirology. 1978;10(1):32–39. doi: 10.1159/000148965. [DOI] [PubMed] [Google Scholar]
- Fairbanks G., Steck T. L., Wallach D. F. Electrophoretic analysis of the major polypeptides of the human erythrocyte membrane. Biochemistry. 1971 Jun 22;10(13):2606–2617. doi: 10.1021/bi00789a030. [DOI] [PubMed] [Google Scholar]
- Feorino P. M., Shore S. L., Reimer C. B. Detection by indirect immunofluorescence of Fc receptors in cells acutely infected with Herpes simplex virus. Int Arch Allergy Appl Immunol. 1977;53(3):222–233. doi: 10.1159/000231756. [DOI] [PubMed] [Google Scholar]
- Heine J. W., Honess R. W., Cassai E., Roizman B. Proteins specified by herpes simplex virus. XII. The virion polypeptides of type 1 strains. J Virol. 1974 Sep;14(3):640–651. doi: 10.1128/jvi.14.3.640-651.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Hubbard A. L., Cohn Z. A. The enzymatic iodination of the red cell membrane. J Cell Biol. 1972 Nov;55(2):390–405. doi: 10.1083/jcb.55.2.390. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Jensenius J. C., Williams A. F. The binding of anti-immunoglobulin antibodies to rat thymocytes and thoracic duct lymphocytes. Eur J Immunol. 1974 Feb;4(2):91–97. doi: 10.1002/eji.1830040207. [DOI] [PubMed] [Google Scholar]
- Keller R., Peitchel R., Goldman J. N., Goldman M. An IgG-Fc receptor induced in cytomegalovirus-infected human fibroblasts. J Immunol. 1976 Mar;116(3):772–777. [PubMed] [Google Scholar]
- Lehner T., Wilton J. M., Shillitoe E. J. Immunological basis for latency, recurrences and putative oncogenicity of herpes simplex virus. Lancet. 1975 Jul 12;2(7924):60–62. doi: 10.1016/s0140-6736(75)90499-7. [DOI] [PubMed] [Google Scholar]
- Manservigi R., Spear P. G., Buchan A. Cell fusion induced by herpes simplex virus is promoted and suppressed by different viral glycoproteins. Proc Natl Acad Sci U S A. 1977 Sep;74(9):3913–3917. doi: 10.1073/pnas.74.9.3913. [DOI] [PMC free article] [PubMed] [Google Scholar]
- McTaggart S. P., Burns W. H., White D. O., Jackson D. C. Fc receptors induced by herpes simplex virus. I. Biologic and biochemical properties. J Immunol. 1978 Aug;121(2):726–730. [PubMed] [Google Scholar]
- NISONOFF A. ENZYMATIC DIGESTION OF RABBIT GAMMA GLOBULIN AND ANTIBODY AND CHROMATOGRAPHY OF DIGESTION PRODUCTS. Methods Med Res. 1964;10:134–141. [PubMed] [Google Scholar]
- Nakamura Y., Costa J., Tralka T. S., Yee C. L., Rabson A. S. Properties of the cell surface Fc-receptor induced by herpes simplex virus. J Immunol. 1978 Sep;121(3):1128–1131. [PubMed] [Google Scholar]
- Rahman A. A., Teschner M., Sethi K. K., Brandis H. Appearance of IgG (Fc) receptor(s) on cultured human fibroblasts infected with human cytomegalovirus. J Immunol. 1976 Jul;117(1):253–258. [PubMed] [Google Scholar]
- Ruyechan W. T., Morse L. S., Knipe D. M., Roizman B. Molecular genetics of herpes simplex virus. II. Mapping of the major viral glycoproteins and of the genetic loci specifying the social behavior of infected cells. J Virol. 1979 Feb;29(2):677–697. doi: 10.1128/jvi.29.2.677-697.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Sakuma S., Furukawa T., Plotkin S. A. The characterization of IgG receptor induced by human cytomegalovirus. Proc Soc Exp Biol Med. 1977 Jun;155(2):168–172. doi: 10.3181/00379727-155-39767. [DOI] [PubMed] [Google Scholar]
- Sarmiento M., Haffey M., Spear P. G. Membrane proteins specified by herpes simplex viruses. III. Role of glycoprotein VP7(B2) in virion infectivity. J Virol. 1979 Mar;29(3):1149–1158. doi: 10.1128/jvi.29.3.1149-1158.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Sarmiento M., Spear P. G. Membrane proteins specified by herpes simplex viruses. IV. Conformation of the virion glycoprotein designated VP7(B2). J Virol. 1979 Mar;29(3):1159–1167. doi: 10.1128/jvi.29.3.1159-1167.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Shimizu Y. Modification of host cell membrane after herpes simplex virus infection. Arch Gesamte Virusforsch. 1971;33(3):338–346. doi: 10.1007/BF01254690. [DOI] [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]
- WATKINS J. F. ADSORPTION OF SENSITIZED SHEEP ERYTHROCYTES TO HELA CELLS INFECTED WITH HERPES SIMPLEX VIRUS. Nature. 1964 Jun 27;202:1364–1365. doi: 10.1038/2021364a0. [DOI] [PubMed] [Google Scholar]
- Watkins J. F. The relationship of the herpes simplex haemadsorption phenomenon to the virus growth cycle. Virology. 1965 Aug;26(4):746–753. [PubMed] [Google Scholar]
- Westmoreland D., St Jeor S., Rapp F. The development by cytomegalovirus-infected cells of binding affinity for normal human immunoglobulin. J Immunol. 1976 Jun;116(6):1566–1570. [PubMed] [Google Scholar]
- Westmoreland D., Watkins J. F. The IgG receptor induced by herpes simplex virus: studies using radioiodinated IgG. J Gen Virol. 1974 Jul;24(1):167–178. doi: 10.1099/0022-1317-24-1-167. [DOI] [PubMed] [Google Scholar]
- Yasuda J., Milgrom F. Hemadsorption by herpes simplex-infected cell cultures. Int Arch Allergy Appl Immunol. 1968;33(2):151–170. doi: 10.1159/000229985. [DOI] [PubMed] [Google Scholar]