Skip to main content
NCBI home page
Journal of Virology logoLink to Journal of Virology
. 1991 Nov;65(11):6137–6143. doi: 10.1128/jvi.65.11.6137-6143.1991

Identification of cell membrane proteins that bind visna virus.

S E Crane 1, J Buzy 1, J E Clements 1
PMCID: PMC250296  PMID: 1656089

Abstract

Visna virus infects cells of ovine origin by attaching to a cell surface receptor via its envelope glycoprotein. The identity of the visna virus receptor is not known. To identify the molecule responsible for binding the virus to target cells, virus overlay protein blot assays were used to examine the molecular weights of cell surface molecules which bind purified virus. Molecules on the surface of goat synovial membrane (GSM) cells and sheep choroid plexus (SCP) cells of approximately 15, 30, and 50 kDa bound to visna virus. The binding of visna virus to these proteins was reduced by preincubating virus with neutralizing antibodies. 125I-labeled cell membrane preparations of GSM and SCP cells were used to affinity purify these virus-binding proteins. These proteins were analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and had molecular masses of 15, 30, and 50 kDa. Antibodies to the 50-kDa protein bound to the surface of both live SCP and GSM cells in immunofluorescence assays. In addition, antibodies to the 50-kDa protein blocked the binding of [35S]methionine-labeled visna virus to SCP cells in culture. Antibodies raised against the 15- and 30-kDa proteins did not block virus binding to cells. The blocking activity of antibody of the 50-kDa protein provided data that this protein is the molecule which visna virus recognizes and binds to on the surface of target cells.

Full text

PDF
6137

Images in this article

6139Image
on p.6139
6139Image
on p.6139
6140Image
on p.6140
6140Image
on p.6140
6142Image
on p.6142

Selected References

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

  1. Acuto O., Hussey R. E., Fitzgerald K. A., Protentis J. P., Meuer S. C., Schlossman S. F., Reinherz E. L. The human T cell receptor: appearance in ontogeny and biochemical relationship of alpha and beta subunits on IL-2 dependent clones and T cell tumors. Cell. 1983 Oct;34(3):717–726. doi: 10.1016/0092-8674(83)90528-7. [DOI] [PubMed] [Google Scholar]
  2. Boyle J. F., Weismiller D. G., Holmes K. V. Genetic resistance to mouse hepatitis virus correlates with absence of virus-binding activity on target tissues. J Virol. 1987 Jan;61(1):185–189. doi: 10.1128/jvi.61.1.185-189.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Choppin P. W., Scheid A. The role of viral glycoproteins in adsorption, penetration, and pathogenicity of viruses. Rev Infect Dis. 1980 Jan-Feb;2(1):40–61. doi: 10.1093/clinids/2.1.40. [DOI] [PubMed] [Google Scholar]
  4. Cork L. C., Hadlow W. J., Crawford T. B., Gorham J. R., Piper R. C. Infectious leukoencephalomyelitis of young goats. J Infect Dis. 1974 Feb;129(2):134–141. doi: 10.1093/infdis/129.2.134. [DOI] [PubMed] [Google Scholar]
  5. Crane S. E., Clements J. E., Narayan O. Separate epitopes in the envelope of visna virus are responsible for fusion and neutralization: biological implications for anti-fusion antibodies in limiting virus replication. J Virol. 1988 Aug;62(8):2680–2685. doi: 10.1128/jvi.62.8.2680-2685.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Creutz C. E., Zaks W. J., Hamman H. C., Crane S., Martin W. H., Gould K. L., Oddie K. M., Parsons S. J. Identification of chromaffin granule-binding proteins. Relationship of the chromobindins to calelectrin, synhibin, and the tyrosine kinase substrates p35 and p36. J Biol Chem. 1987 Feb 5;262(4):1860–1868. [PubMed] [Google Scholar]
  7. Frade R., Barel M., Ehlin-Henriksson B., Klein G. gp140, the C3d receptor of human B lymphocytes, is also the Epstein-Barr virus receptor. Proc Natl Acad Sci U S A. 1985 Mar;82(5):1490–1493. doi: 10.1073/pnas.82.5.1490. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Greve J. M., Davis G., Meyer A. M., Forte C. P., Yost S. C., Marlor C. W., Kamarck M. E., McClelland A. The major human rhinovirus receptor is ICAM-1. Cell. 1989 Mar 10;56(5):839–847. doi: 10.1016/0092-8674(89)90688-0. [DOI] [PubMed] [Google Scholar]
  9. Jolly P. E., Huso D. L., Sheffer D., Narayan O. Modulation of lentivirus replication by antibodies: Fc portion of immunoglobulin molecule is essential for enhancement of binding, internalization, and neutralization of visna virus in macrophages. J Virol. 1989 Apr;63(4):1811–1813. doi: 10.1128/jvi.63.4.1811-1813.1989. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Jolly P. E., Narayan O. Evidence for interference, coinfections, and intertypic virus enhancement of infection by ovine-caprine lentiviruses. J Virol. 1989 Nov;63(11):4682–4688. doi: 10.1128/jvi.63.11.4682-4688.1989. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Kennedy-Stoskopf S., Narayan O. Neutralizing antibodies to visna lentivirus: mechanism of action and possible role in virus persistence. J Virol. 1986 Jul;59(1):37–44. doi: 10.1128/jvi.59.1.37-44.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Lifson J. D., Hwang K. M., Nara P. L., Fraser B., Padgett M., Dunlop N. M., Eiden L. E. Synthetic CD4 peptide derivatives that inhibit HIV infection and cytopathicity. Science. 1988 Aug 5;241(4866):712–716. doi: 10.1126/science.2969619. [DOI] [PubMed] [Google Scholar]
  13. 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]
  14. Maddon P. J., McDougal J. S., Clapham P. R., Dalgleish A. G., Jamal S., Weiss R. A., Axel R. HIV infection does not require endocytosis of its receptor, CD4. Cell. 1988 Sep 9;54(6):865–874. doi: 10.1016/s0092-8674(88)91241-x. [DOI] [PubMed] [Google Scholar]
  15. Markwell M. A., Haas S. M., Bieber L. L., Tolbert N. E. A modification of the Lowry procedure to simplify protein determination in membrane and lipoprotein samples. Anal Biochem. 1978 Jun 15;87(1):206–210. doi: 10.1016/0003-2697(78)90586-9. [DOI] [PubMed] [Google Scholar]
  16. McDougal J. S., Kennedy M. S., Sligh J. M., Cort S. P., Mawle A., Nicholson J. K. Binding of HTLV-III/LAV to T4+ T cells by a complex of the 110K viral protein and the T4 molecule. Science. 1986 Jan 24;231(4736):382–385. doi: 10.1126/science.3001934. [DOI] [PubMed] [Google Scholar]
  17. Mendelsohn C. L., Wimmer E., Racaniello V. R. Cellular receptor for poliovirus: molecular cloning, nucleotide sequence, and expression of a new member of the immunoglobulin superfamily. Cell. 1989 Mar 10;56(5):855–865. doi: 10.1016/0092-8674(89)90690-9. [DOI] [PubMed] [Google Scholar]
  18. Narayan O., Clements J. E. Biology and pathogenesis of lentiviruses. J Gen Virol. 1989 Jul;70(Pt 7):1617–1639. doi: 10.1099/0022-1317-70-7-1617. [DOI] [PubMed] [Google Scholar]
  19. Narayan O., Clements J. E., Griffin D. E., Wolinsky J. S. Neutralizing antibody spectrum determines the antigenic profiles of emerging mutants of visna virus. Infect Immun. 1981 Jun;32(3):1045–1050. doi: 10.1128/iai.32.3.1045-1050.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Narayan O., Clements J. E., Strandberg J. D., Cork L. C., Griffin D. E. Biological characterization of the virus causing leukoencephalitis and arthritis in goats. J Gen Virol. 1980 Sep;50(1):69–79. doi: 10.1099/0022-1317-50-1-69. [DOI] [PubMed] [Google Scholar]
  21. Narayan O., Griffin D. E., Chase J. Antigenic shift of visna virus in persistently infected sheep. Science. 1977 Jul 22;197(4301):376–378. doi: 10.1126/science.195339. [DOI] [PubMed] [Google Scholar]
  22. Narayan O., Griffin D. E., Clements J. E. Virus mutation during 'slow infection': temporal development and characterization of mutants of visna virus recovered from sheep. J Gen Virol. 1978 Nov;41(2):343–352. doi: 10.1099/0022-1317-41-2-343. [DOI] [PubMed] [Google Scholar]
  23. Pyper J. M., Clements J. E., Molineaux S. M., Narayan O. Genetic variation among lentiviruses: homology between visna virus and caprine arthritis-encephalitis virus is confined to the 5' gag-pol region and a small portion of the env gene. J Virol. 1984 Sep;51(3):713–721. doi: 10.1128/jvi.51.3.713-721.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. SIGURDSSON B., PALSSON P., GRIMSSON H. Visna, a demyelinating transmissible disease of sheep. J Neuropathol Exp Neurol. 1957 Jul;16(3):389–403. doi: 10.1097/00005072-195707000-00010. [DOI] [PubMed] [Google Scholar]
  25. Sattentau Q. J., Weiss R. A. The CD4 antigen: physiological ligand and HIV receptor. Cell. 1988 Mar 11;52(5):631–633. doi: 10.1016/0092-8674(88)90397-2. [DOI] [PubMed] [Google Scholar]
  26. Smith D. H., Byrn R. A., Marsters S. A., Gregory T., Groopman J. E., Capon D. J. Blocking of HIV-1 infectivity by a soluble, secreted form of the CD4 antigen. Science. 1987 Dec 18;238(4834):1704–1707. doi: 10.1126/science.3500514. [DOI] [PubMed] [Google Scholar]
  27. Stanley J., Bhaduri L. M., Narayan O., Clements J. E. Topographical rearrangements of visna virus envelope glycoprotein during antigenic drift. J Virol. 1987 Apr;61(4):1019–1028. doi: 10.1128/jvi.61.4.1019-1028.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  28. Staunton D. E., Merluzzi V. J., Rothlein R., Barton R., Marlin S. D., Springer T. A. A cell adhesion molecule, ICAM-1, is the major surface receptor for rhinoviruses. Cell. 1989 Mar 10;56(5):849–853. doi: 10.1016/0092-8674(89)90689-2. [DOI] [PubMed] [Google Scholar]
  29. THORMAR H. The growth cycle of visna virus in monolayer cultures of sheep cells. Virology. 1963 Mar;19:273–278. doi: 10.1016/0042-6822(63)90064-3. [DOI] [PubMed] [Google Scholar]

Articles from Journal of Virology are provided here courtesy of American Society for Microbiology (ASM)

RESOURCES