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. 1985 Aug;55(2):483–488. doi: 10.1128/jvi.55.2.483-488.1985

Potent neutralizing activity associated with anti-glycoprotein D specificity among monoclonal antibodies selected for binding to herpes simplex virions.

M F Para, M L Parish, A G Noble, P G Spear
PMCID: PMC254957  PMID: 2991571

Abstract

Thirty-three monoclonal antibodies were selected for ability to bind to purified virions of herpes simplex virus and were shown by immunoprecipitation to react with one or another of the envelope glycoproteins. Only six of these antibodies exhibited potent neutralizing activity, and all six were specific for glycoprotein D. Two other anti-glycoprotein D antibodies and 25 antibodies specific for four other viral glycoproteins had much less potent, if any, neutralizing activity.

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Selected References

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  1. Balachandran N., Bacchetti S., Rawls W. E. Protection against lethal challenge of BALB/c mice by passive transfer of monoclonal antibodies to five glycoproteins of herpes simplex virus type 2. Infect Immun. 1982 Sep;37(3):1132–1137. doi: 10.1128/iai.37.3.1132-1137.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Balachandran N., Harnish D., Rawls W. E., Bacchetti S. Glycoproteins of herpes simplex virus type 2 as defined by monoclonal antibodies. J Virol. 1982 Oct;44(1):344–355. doi: 10.1128/jvi.44.1.344-355.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Baucke R. B., Spear P. G. Membrane proteins specified by herpes simplex viruses. V. Identification of an Fc-binding glycoprotein. J Virol. 1979 Dec;32(3):779–789. doi: 10.1128/jvi.32.3.779-789.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Buckmaster E. A., Gompels U., Minson A. Characterisation and physical mapping of an HSV-1 glycoprotein of approximately 115 X 10(3) molecular weight. Virology. 1984 Dec;139(2):408–413. doi: 10.1016/0042-6822(84)90387-8. [DOI] [PubMed] [Google Scholar]
  5. 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]
  6. Cohen G. H., Dietzschold B., Ponce de Leon M., Long D., Golub E., Varrichio A., Pereira L., Eisenberg R. J. Localization and synthesis of an antigenic determinant of herpes simplex virus glycoprotein D that stimulates the production of neutralizing antibody. J Virol. 1984 Jan;49(1):102–108. doi: 10.1128/jvi.49.1.102-108.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. 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]
  8. 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]
  9. Dietzschold B., Eisenberg R. J., Ponce de Leon M., Golub E., Hudecz F., Varrichio A., Cohen G. H. Fine structure analysis of type-specific and type-common antigenic sites of herpes simplex virus glycoprotein D. J Virol. 1984 Nov;52(2):431–435. doi: 10.1128/jvi.52.2.431-435.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Eberle R., Courtney R. J. Preparation and characterization of specific antisera to individual glycoprotein antigens comprising the major glycoprotein region of herpes simplex virus type 1. J Virol. 1980 Sep;35(3):902–917. doi: 10.1128/jvi.35.3.902-917.1980. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Eisenberg R. J., Long D., Pereira L., Hampar B., Zweig M., Cohen G. H. Effect of monoclonal antibodies on limited proteolysis of native glycoprotein gD of herpes simplex virus type 1. J Virol. 1982 Feb;41(2):478–488. doi: 10.1128/jvi.41.2.478-488.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Eisenberg R. J., Long D., Ponce de Leon M., Matthews J. T., Spear P. G., Gibson M. G., Lasky L. A., Berman P., Golub E., Cohen G. H. Localization of epitopes of herpes simplex virus type 1 glycoprotein D. J Virol. 1985 Feb;53(2):634–644. doi: 10.1128/jvi.53.2.634-644.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Eisenberg R. J., Ponce de Leon M., Pereira L., Long D., Cohen G. H. Purification of glycoprotein gD of herpes simplex virus types 1 and 2 by use of monoclonal antibody. J Virol. 1982 Mar;41(3):1099–1104. doi: 10.1128/jvi.41.3.1099-1104.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Ejercito P. M., Kieff E. D., Roizman B. Characterization of herpes simplex virus strains differing in their effects on social behaviour of infected cells. J Gen Virol. 1968 May;2(3):357–364. doi: 10.1099/0022-1317-2-3-357. [DOI] [PubMed] [Google Scholar]
  15. Ey P. L., Prowse S. J., Jenkin C. R. Isolation of pure IgG1, IgG2a and IgG2b immunoglobulins from mouse serum using protein A-sepharose. Immunochemistry. 1978 Jul;15(7):429–436. doi: 10.1016/0161-5890(78)90070-6. [DOI] [PubMed] [Google Scholar]
  16. Fuller A. O., Spear P. G. Specificities of monoclonal and polyclonal antibodies that inhibit adsorption of herpes simplex virus to cells and lack of inhibition by potent neutralizing antibodies. J Virol. 1985 Aug;55(2):475–482. doi: 10.1128/jvi.55.2.475-482.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Holland T. C., Marlin S. D., Levine M., Glorioso J. Antigenic variants of herpes simplex virus selected with glycoprotein-specific monoclonal antibodies. J Virol. 1983 Feb;45(2):672–682. doi: 10.1128/jvi.45.2.672-682.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Honess R. W., Watson D. H. Herpes simplex virus-specific polypeptides studied by polyacrylamide gel electrophoresis of immune precipitates. J Gen Virol. 1974 Feb;22(2):171–185. doi: 10.1099/0022-1317-22-2-171. [DOI] [PubMed] [Google Scholar]
  19. Kronvall G., Grey H. M., Williams R. C., Jr Protein A reactivity with mouse immunoglobulins. Structural relationship between some mouse and human immunoglobulins. J Immunol. 1970 Nov;105(5):1116–1123. [PubMed] [Google Scholar]
  20. Marsden H. S., Buckmaster A., Palfreyman J. W., Hope R. G., Minson A. C. Characterization of the 92,000-dalton glycoprotein induced by herpes simplex virus type 2. J Virol. 1984 May;50(2):547–554. doi: 10.1128/jvi.50.2.547-554.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Marsden H. S., Stow N. D., Preston V. G., Timbury M. C., Wilkie N. M. Physical mapping of herpes simplex virus-induced polypeptides. J Virol. 1978 Nov;28(2):624–642. doi: 10.1128/jvi.28.2.624-642.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. McKearn T. J., Sarmiento M., Weiss A., Stuart F. P., Fitch F. W. Selective suppression of reactivity to rat histocompatibility antigens by hybridoma antibodies. Curr Top Microbiol Immunol. 1978;81:61–65. doi: 10.1007/978-3-642-67448-8_10. [DOI] [PubMed] [Google Scholar]
  23. Noble A. G., Lee G. T., Sprague R., Parish M. L., Spear P. G. Anti-gD monoclonal antibodies inhibit cell fusion induced by herpes simplex virus type 1. Virology. 1983 Aug;129(1):218–224. doi: 10.1016/0042-6822(83)90409-9. [DOI] [PubMed] [Google Scholar]
  24. Para M. F., Baucke R. B., Spear P. G. Glycoprotein gE of herpes simplex virus type 1: effects of anti-gE on virion infectivity and on virus-induced fc-binding receptors. J Virol. 1982 Jan;41(1):129–136. doi: 10.1128/jvi.41.1.129-136.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Para M. F., Zezulak K. M., Conley A. J., Weinberger M., Snitzer K., Spear P. G. Use of monoclonal antibodies against two 75,000-molecular-weight glycoproteins specified by herpes simplex virus type 2 in glycoprotein identification and gene mapping. J Virol. 1983 Mar;45(3):1223–1227. doi: 10.1128/jvi.45.3.1223-1227.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  26. Pereira L., Dondero D. V., Gallo D., Devlin V., Woodie J. D. Serological analysis of herpes simplex virus types 1 and 2 with monoclonal antibodies. Infect Immun. 1982 Jan;35(1):363–367. doi: 10.1128/iai.35.1.363-367.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  27. Pereira L., Dondero D., Norrild B., Roizman B. Differential immunologic reactivity and processing of glycoproteins gA and gB of herpes simplex virus types 1 and 2 made in Vero and HEp-2 cells. Proc Natl Acad Sci U S A. 1981 Aug;78(8):5202–5206. doi: 10.1073/pnas.78.8.5202. [DOI] [PMC free article] [PubMed] [Google Scholar]
  28. 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]
  29. Powell K. L., Buchan A., Sim C., Watson D. H. Type-specific protein in herpes simplex virus envelope reacts with neutralising antibody. Nature. 1974 May 24;249(455):360–361. doi: 10.1038/249360a0. [DOI] [PubMed] [Google Scholar]
  30. Rector J. T., Lausch R. N., Oakes J. E. Use of monoclonal antibodies for analysis of antibody-dependent immunity to ocular herpes simplex virus type 1 infection. Infect Immun. 1982 Oct;38(1):168–174. doi: 10.1128/iai.38.1.168-174.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  31. Roizman B., Norrild B., Chan C., Pereira L. Identification and preliminary mapping with monoclonal antibodies of a herpes simplex virus 2 glycoprotein lacking a known type 1 counterpart. Virology. 1984 Feb;133(1):242–247. doi: 10.1016/0042-6822(84)90447-1. [DOI] [PubMed] [Google Scholar]
  32. Showalter S. D., Zweig M., Hampar B. Monoclonal antibodies to herpes simplex virus type 1 proteins, including the immediate-early protein ICP 4. Infect Immun. 1981 Dec;34(3):684–692. doi: 10.1128/iai.34.3.684-692.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
  33. Shulman M., Wilde C. D., Köhler G. A better cell line for making hybridomas secreting specific antibodies. Nature. 1978 Nov 16;276(5685):269–270. doi: 10.1038/276269a0. [DOI] [PubMed] [Google Scholar]
  34. Sim C., Watson D. H. The role of type specific and cross reacting structural antigens in the neutralization of herpes simplex virus types 1 and 2. J Gen Virol. 1973 May;19(2):217–233. doi: 10.1099/0022-1317-19-2-217. [DOI] [PubMed] [Google Scholar]
  35. Spear P. G., Roizman B. Proteins specified by herpes simplex virus. V. Purification and structural proteins of the herpesvirion. J Virol. 1972 Jan;9(1):143–159. doi: 10.1128/jvi.9.1.143-159.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
  36. Vestergaard B. F., Norrild B. Crossed immunoelectrophoretic analysis and viral neutralizing activity of five monospecific antisera against five different herpes simplex virus glycoproteins. IARC Sci Publ. 1978;(24 Pt 1):225–234. [PubMed] [Google Scholar]
  37. Watson D. H., Wildy P. The preparation of 'monoprecipitin' antisera to herpes virus specific antigens. J Gen Virol. 1969 Mar;4(2):163–168. doi: 10.1099/0022-1317-4-2-163. [DOI] [PubMed] [Google Scholar]
  38. Zezulak K. M., Spear P. G. Characterization of a herpes simplex virus type 2 75,000-molecular-weight glycoprotein antigenically related to herpes simplex virus type 1 glycoprotein C. J Virol. 1983 Sep;47(3):553–562. doi: 10.1128/jvi.47.3.553-562.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]

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