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. 1991 Sep;65(9):5124–5128. doi: 10.1128/jvi.65.9.5124-5128.1991

Anti-idiotype antibodies that mimic gp86 of human cytomegalovirus inhibit viral fusion but not attachment.

S Keay 1, B Baldwin 1
PMCID: PMC248982  PMID: 1651427

Abstract

Human cytomegalovirus (CMV) infects cells by sequential processes involving attachment, fusion with the cell membrane, and penetration of the capsid. We used two monoclonal anti-idiotype that mimic one of the CMV envelope glycoproteins, gp86, to study its role in the early phases of CMV infection. Neither of two such antibodies inhibited virus binding to human embryonic lung (HEL) fibroblasts; however, both antibodies inhibited the fusion of CMV with HEL cells, as measured by an assay in which viral envelope is labeled with a fluorescent amphiphile (octadecyl rhodamine B chloride, or R18), resulting in increased fluorescence during fusion of virus with the cell membrane. Because these anti-idiotype antibodies were shown previously to bind to specific receptors on HEL cell membranes, these findings suggest that both gp86 and its cell membrane receptor may function in the fusion of human CMV with HEL cells.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Adlish J. D., Lahijani R. S., St Jeor S. C. Identification of a putative cell receptor for human cytomegalovirus. Virology. 1990 Jun;176(2):337–345. doi: 10.1016/0042-6822(90)90003-a. [DOI] [PubMed] [Google Scholar]
  2. Ali M. A., Butcher M., Ghosh H. P. Expression and nuclear envelope localization of biologically active fusion glycoprotein gB of herpes simplex virus in mammalian cells using cloned DNA. Proc Natl Acad Sci U S A. 1987 Aug;84(16):5675–5679. doi: 10.1073/pnas.84.16.5675. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Bidlack J. M., Mabie P. C. Preparation of Fab fragments from a mouse monoclonal IgM. J Immunol Methods. 1986 Jul 24;91(2):157–162. doi: 10.1016/0022-1759(86)90473-4. [DOI] [PubMed] [Google Scholar]
  4. Campadelli-Fiume G., Arsenakis M., Farabegoli F., Roizman B. Entry of herpes simplex virus 1 in BJ cells that constitutively express viral glycoprotein D is by endocytosis and results in degradation of the virus. J Virol. 1988 Jan;62(1):159–167. doi: 10.1128/jvi.62.1.159-167.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Campadelli-Fiume G., Stirpe D., Boscaro A., Avitabile E., Foá-Tomasi L., Barker D., Roizman B. Glycoprotein C-dependent attachment of herpes simplex virus to susceptible cells leading to productive infection. Virology. 1990 Sep;178(1):213–222. doi: 10.1016/0042-6822(90)90396-9. [DOI] [PubMed] [Google Scholar]
  6. Fuller A. O., Santos R. E., Spear P. G. Neutralizing antibodies specific for glycoprotein H of herpes simplex virus permit viral attachment to cells but prevent penetration. J Virol. 1989 Aug;63(8):3435–3443. doi: 10.1128/jvi.63.8.3435-3443.1989. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Gompels U., Minson A. The properties and sequence of glycoprotein H of herpes simplex virus type 1. Virology. 1986 Sep;153(2):230–247. doi: 10.1016/0042-6822(86)90026-7. [DOI] [PubMed] [Google Scholar]
  8. Grundy J. E., McKeating J. A., Ward P. J., Sanderson A. R., Griffiths P. D. Beta 2 microglobulin enhances the infectivity of cytomegalovirus and when bound to the virus enables class I HLA molecules to be used as a virus receptor. J Gen Virol. 1987 Mar;68(Pt 3):793–803. doi: 10.1099/0022-1317-68-3-793. [DOI] [PubMed] [Google Scholar]
  9. Hoekstra D., Klappe K. Sendai virus-erythrocyte membrane interaction: quantitative and kinetic analysis of viral binding, dissociation, and fusion. J Virol. 1986 Apr;58(1):87–95. doi: 10.1128/jvi.58.1.87-95.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Hoekstra D., Kok J. W. Entry mechanisms of enveloped viruses. Implications for fusion of intracellular membranes. Biosci Rep. 1989 Jun;9(3):273–305. doi: 10.1007/BF01114682. [DOI] [PubMed] [Google Scholar]
  11. Hoekstra D., de Boer T., Klappe K., Wilschut J. Fluorescence method for measuring the kinetics of fusion between biological membranes. Biochemistry. 1984 Nov 20;23(24):5675–5681. doi: 10.1021/bi00319a002. [DOI] [PubMed] [Google Scholar]
  12. Keay S., Merigan T. C., Rasmussen L. Identification of cell surface receptors for the 86-kilodalton glycoprotein of human cytomegalovirus. Proc Natl Acad Sci U S A. 1989 Dec;86(24):10100–10103. doi: 10.1073/pnas.86.24.10100. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Keay S., Rasmussen L., Merigan T. C. Syngeneic monoclonal anti-idiotype antibodies that bear the internal image of a human cytomegalovirus neutralization epitope. J Immunol. 1988 Feb 1;140(3):944–948. [PubMed] [Google Scholar]
  14. Keller P. M., Davison A. J., Lowe R. S., Riemen M. W., Ellis R. W. Identification and sequence of the gene encoding gpIII, a major glycoprotein of varicella-zoster virus. Virology. 1987 Apr;157(2):526–533. doi: 10.1016/0042-6822(87)90295-9. [DOI] [PubMed] [Google Scholar]
  15. Kim Y. D., Hu R. C., Mimms L. T. Determination of intrinsic association constant of mouse monoclonal IgM antibody to human hepatitis B surface antigen. J Immunol Methods. 1989 Jun 2;120(1):9–15. doi: 10.1016/0022-1759(89)90282-2. [DOI] [PubMed] [Google Scholar]
  16. Loyter A., Citovsky V., Blumenthal R. The use of fluorescence dequenching measurements to follow viral membrane fusion events. Methods Biochem Anal. 1988;33:129–164. doi: 10.1002/9780470110546.ch4. [DOI] [PubMed] [Google Scholar]
  17. Maddon P. J., Dalgleish A. G., McDougal J. S., Clapham P. R., Weiss R. A., Axel R. The T4 gene encodes the AIDS virus receptor and is expressed in the immune system and the brain. Cell. 1986 Nov 7;47(3):333–348. doi: 10.1016/0092-8674(86)90590-8. [DOI] [PubMed] [Google Scholar]
  18. Marsh M., Helenius A. Virus entry into animal cells. Adv Virus Res. 1989;36:107–151. doi: 10.1016/S0065-3527(08)60583-7. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Mendelsohn C., Johnson B., Lionetti K. A., Nobis P., Wimmer E., Racaniello V. R. Transformation of a human poliovirus receptor gene into mouse cells. Proc Natl Acad Sci U S A. 1986 Oct;83(20):7845–7849. doi: 10.1073/pnas.83.20.7845. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Miller F. A., Dixon G. J., Arnett G., Dice J. R., Rightsel W. A., Schabel F. M., Jr, McLean I. W., Jr Antiviral activity of carbobenzosy di- and tripeptides on measles virus. Appl Microbiol. 1968 Oct;16(10):1489–1496. doi: 10.1128/am.16.10.1489-1496.1968. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Miller N., Hutt-Fletcher L. M. A monoclonal antibody to glycoprotein gp85 inhibits fusion but not attachment of Epstein-Barr virus. J Virol. 1988 Jul;62(7):2366–2372. doi: 10.1128/jvi.62.7.2366-2372.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Nemerow G. R., Cooper N. R. Early events in the infection of human B lymphocytes by Epstein-Barr virus: the internalization process. Virology. 1984 Jan 15;132(1):186–198. doi: 10.1016/0042-6822(84)90102-8. [DOI] [PubMed] [Google Scholar]
  23. Nemerow G. R., Mold C., Schwend V. K., Tollefson V., Cooper N. R. Identification of gp350 as the viral glycoprotein mediating attachment of Epstein-Barr virus (EBV) to the EBV/C3d receptor of B cells: sequence homology of gp350 and C3 complement fragment C3d. J Virol. 1987 May;61(5):1416–1420. doi: 10.1128/jvi.61.5.1416-1420.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. Nemerow G. R., Wolfert R., McNaughton M. E., Cooper N. R. Identification and characterization of the Epstein-Barr virus receptor on human B lymphocytes and its relationship to the C3d complement receptor (CR2). J Virol. 1985 Aug;55(2):347–351. doi: 10.1128/jvi.55.2.347-351.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Nir S., Klappe K., Hoekstra D. Mass action analysis of kinetics and extent of fusion between Sendai virus and phospholipid vesicles. Biochemistry. 1986 Dec 16;25(25):8261–8266. doi: 10.1021/bi00373a020. [DOI] [PubMed] [Google Scholar]
  26. Norrby E. The effect of a carbobenzoxy tripeptide on the biological activities of measles virus. Virology. 1971 Jun;44(3):599–608. doi: 10.1016/0042-6822(71)90374-6. [DOI] [PubMed] [Google Scholar]
  27. Rasmussen L. E., Nelson R. M., Kelsall D. C., Merigan T. C. Murine monoclonal antibody to a single protein neutralizes the infectivity of human cytomegalovirus. Proc Natl Acad Sci U S A. 1984 Feb;81(3):876–880. doi: 10.1073/pnas.81.3.876. [DOI] [PMC free article] [PubMed] [Google Scholar]
  28. Richardson C. D., Choppin P. W. Oligopeptides that specifically inhibit membrane fusion by paramyxoviruses: studies on the site of action. Virology. 1983 Dec;131(2):518–532. doi: 10.1016/0042-6822(83)90517-2. [DOI] [PubMed] [Google Scholar]
  29. Seigneurin J. M., Vuillaume M., Lenoir G., De-Thé G. Replication of Epstein-Barr virus: ultrastructural and immunofluorescent studies of P3HR1-superinfected Raji cells. J Virol. 1977 Dec;24(3):836–845. doi: 10.1128/jvi.24.3.836-845.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
  30. Tanner J., Weis J., Fearon D., Whang Y., Kieff E. Epstein-Barr virus gp350/220 binding to the B lymphocyte C3d receptor mediates adsorption, capping, and endocytosis. Cell. 1987 Jul 17;50(2):203–213. doi: 10.1016/0092-8674(87)90216-9. [DOI] [PubMed] [Google Scholar]
  31. Taylor H. P., Cooper N. R. The human cytomegalovirus receptor on fibroblasts is a 30-kilodalton membrane protein. J Virol. 1990 Jun;64(6):2484–2490. doi: 10.1128/jvi.64.6.2484-2490.1990. [DOI] [PMC free article] [PubMed] [Google Scholar]
  32. Varsanyi T. M., Jörnvall H., Norrby E. Isolation and characterization of the measles virus F1 polypeptide: comparison with other paramyxovirus fusion proteins. Virology. 1985 Nov;147(1):110–117. doi: 10.1016/0042-6822(85)90231-4. [DOI] [PubMed] [Google Scholar]
  33. Wells A., Koide N., Klein G. Two large virion envelope glycoproteins mediate Epstein-Barr virus binding to receptor-positive cells. J Virol. 1982 Jan;41(1):286–297. doi: 10.1128/jvi.41.1.286-297.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  34. WuDunn D., Spear P. G. Initial interaction of herpes simplex virus with cells is binding to heparan sulfate. J Virol. 1989 Jan;63(1):52–58. doi: 10.1128/jvi.63.1.52-58.1989. [DOI] [PMC free article] [PubMed] [Google Scholar]

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