Skip to main content
SpringerLink
Log in
Book cover

Vaccinia Virus and Poxvirology pp 219–242Cite as

Interaction Analysis of Viral Cytokine-Binding Proteins Using Surface Plasmon Resonance

  • Protocol

  • 1527 Accesses

Part of the book series: Methods in Molecular Biology ((MIMB,volume 269))

Abstract

Surface plasmon resonance (SPR) biosensors have become an increasingly popular technology for characterizing the protein-protein interactions of virus-host interactions. Various studies have exploited the versatility of SPR to probe the interaction between virus and host components, including constituents of virus particles and host cellular receptors, as well as interactions between viral proteins and host immune molecules. This chapter describes basic procedures for employing SPR to study the interaction between poxvirus proteins and host immune-signaling proteins. We also identify how this methodology may be adapted toward other applications relevant in the study of poxvirus-host interactions.

This is a preview of subscription content, log in via an institution.

Protocol
USD   49.95
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
eBook
USD   109.00
Price excludes VAT (USA)
  • Available as EPUB and PDF
  • Read on any device
  • Instant download
  • Own it forever
Softcover Book
USD   139.00
Price excludes VAT (USA)
  • Compact, lightweight edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info

Tax calculation will be finalised at checkout

Purchases are for personal use only

Learn about institutional subscriptions

Springer Nature is developing a new tool to find and evaluate Protocols. Learn more

References

  1. Seet, B. T., Johnston, J., Brunetti, C., Barrett, J., Everett, H., Cameron, C., et al. (2002) Poxviruses and immune evasion. Annu. Rev. Immunol. 21, 377–423.

    Article  Google Scholar 

  2. McFadden, G., ed. (1995) Viroceptors, Virokines and Related Immune Modulators Encoded by DNA Viruses. R.G. Landes Company, Austin, TX.

    Google Scholar 

  3. Myszka, D. G. (1999) Improving biosensor analysis. J. Mol. Recognit. 12, 279–284.

    Article  PubMed  CAS  Google Scholar 

  4. Rich, R. L. and Myszka, D. G. (2000) Advances in surface plasmon resonance biosensor analysis. Curr. Opin. Biotechnol. 11, 54–61.

    Article  PubMed  CAS  Google Scholar 

  5. Myszka, D. G. and Morton, T. A. (1998) CLAMP: a biosensor kinetic data analysis program. Trends Biochem. Sci. 23, 149–150.

    Article  PubMed  CAS  Google Scholar 

  6. Rich, R. L., Hoth, L. R., Geoghegan, K. F., Brown, T. A., LeMotte, P. K., Simons, S. P., et al. (2002) Kinetic analysis of estrogen receptor/ligand interactions. Proc. Natl. Acad. Sci. USA 99, 8562–8567.

    Article  PubMed  CAS  Google Scholar 

  7. Xiang, Y. and Moss, B. (2001) Correspondence of the functional epitopes of poxvirus and human interleukin-18-binding proteins. J. Virol. 75, 9947–9954.

    Article  PubMed  CAS  Google Scholar 

  8. Smith, C. A., Smith, T. D., Smolak, P. J., Friend, D., Hagen, H., Gerhart, M., et al. (1997) Poxvirus genomes encode a secreted soluble protein that preferentially inhibits b chemokine activity yet lacks sequence homology to known chemokine receptors. Virology 236, 316–327.

    Article  PubMed  CAS  Google Scholar 

  9. Seet, B. T. and McFadden, G. (2002) Viral chemokine binding proteins. J. Leuk. Biol. 72, 24–34.

    CAS  Google Scholar 

  10. Seet, B. T., Barrett, J., Robichaud, J., Shilton, B., Singh, R., and McFadden, G. (2001) Glycosaminoglycan-binding properties of the myxoma virus CC-chemokine inhibitor, M-T1. J. Biol. Chem. 276, 30504–30513.

    Article  PubMed  CAS  Google Scholar 

  11. Tzahar, E., Moyer, J. D., Waterman, H., Barbacci, E. G., Bao, J., Levkowitz, G., et al. (1998) Pathogenic poxviruses reveal viral strategies to exploit the ErbB signaling network. EMBO J. 17, 5948–5963.

    Article  PubMed  CAS  Google Scholar 

  12. Seet, B. T., Singh, R., Paavola, C., Lau, E. K., Handel, T. M., and McFadden, G. (2001) Molecular determinants for CC-chemokine recognition by a poxvirus CC-chemokine inhibitor. Proc. Natl. Acad. Sci. USA 98, 9008–9013.

    Article  PubMed  CAS  Google Scholar 

  13. Beck, C. G., Studer, C., Zuber, J. F., Jachez Demange, B., Manning, U., and Urfer, R. (2001) The viral CC chemokine binding protein vCCI inhibits monocyte chemoattractant protein-1 activity by masking its CCR2B binding site. J. Biol. Chem. 276, 43270–43276.

    Article  PubMed  CAS  Google Scholar 

  14. Ng, A., Tscharke, D. C., Reading, P. C., and Smith, G. L. (2001) The vaccinia virus A41L protein is a soluble 30 kDa glycoprotein that affects virus virulence. J. Gen. Virol. 82, 2095–2105.

    PubMed  CAS  Google Scholar 

  15. Calderara, S., Xiang, Y., and Moss, B. (2001) Orthopoxvirus IL-18 binding proteins: affinities and antagonist activities. Virology 279, 22–26.

    Article  PubMed  CAS  Google Scholar 

  16. Machesky, L. M., Cole, N. B., Moss, B., and Pollard, T. D. (1994) Vaccinia virus expresses a novel profilin with a higher affinity for polyphosphoinositides than actin. Biochem. 33, 10815–10824.

    Article  CAS  Google Scholar 

  17. Loparev, V. N., Parsons, J. M., Knight, J. C., Panus, J. F., Ray, C. A., Buller, R. M., et al. (1998) A third distinct tumor necrosis factor receptor of orthopoxviruses. Proc. Natl. Acad. Sci. USA 95, 3786–3791.

    Article  PubMed  CAS  Google Scholar 

  18. Symons, J. A., Tscharke, D. C., Price, N., and Smith, G. L. (2002) A study of the vaccinia virus interferon-gamma receptor and its contribution to virus virulence. J. Gen. Virol. 83, 1953–1964.

    PubMed  CAS  Google Scholar 

  19. Shi, X., Yao, P., Jose, T., and Gershon, P. (1996) Methyltransferase-specific domains within VP-39, a bifunctional protein that participates in the modification of both mRNA ends. RNA 2, 88–101.

    PubMed  CAS  Google Scholar 

  20. Gershon, P. D. and Khilko, S. (1995) Stable chelating linkage for reversible immobilization of oligohistidine tagged proteins in the BIAcore surface plasmon resonance detector. J. Immunol. Meth. 183, 65–76.

    Article  CAS  Google Scholar 

  21. Alcami, A., Khanna, A., Paul, N. L., and Smith, G. L. (1999) Vaccinia virus strains Lister, USSR and Evans express soluble and cell-surface tumour necrosis factor receptors. J. Gen. Virol. 80, 949–959.

    PubMed  CAS  Google Scholar 

  22. Xiang, Y. and Moss, B. (1999) Identification of human and mouse homologs of the MC51L-53L-54L family of secreted glycoproteins encoded by the Molluscum contagiosum poxvirus. Virology 257, 297–302.

    Article  PubMed  CAS  Google Scholar 

  23. Born, T. L., Morrison, L. A., Esteban, D. J., VandenBos, T., Thebeau, L. G., Chen, N., et al. (2000) A poxvirus protein that binds to and inactivates IL-18, and inhibits NK cell response. J. Immunol. 164, 3246–3254.

    PubMed  CAS  Google Scholar 

  24. Seet, B. T., McCaughan, C. A., Mercer, A., Handel, T., McFadden, G., and Fleming, S. B. (2003) Analysis of a chemokine inhibitor protein encoded by the orf poxvirus: shifting ligand specificity among a family of poxvirus viroceptors. Proc. Natl. Acad. Sci. USA 100, 13137–15142.

    Article  Google Scholar 

  25. Brunetti, C. R., Paulose-Murphy, M., Singh, R., Qin, J., Barrett, J. W., Tardivel, A., et al. (2003) A secreted high-affinity inhibitor of human TNF from Tanapox virus. Proc. Natl. Acad. Sci. USA 100, 4831–4836.

    Article  PubMed  CAS  Google Scholar 

Download references

Author information

Authors and Affiliations

  1. Department of Microbiology and Immunology, The University of Western Ontario and The John P. Robarts Research Institute, London, Ontario, Canada

    Bruce T. Seet

  2. Viral Immunology and Pathogenesis Laboratories, University of Western Ontario and The John P. Robarts Research Institute, London, Ontario, Canada

    Grant McFadden

Authors
  1. Bruce T. Seet
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Grant McFadden
    View author publications

    You can also search for this author in PubMed Google Scholar

Editor information

Editors and Affiliations

  1. Division of Infectious Diseases, University of Pennsylvania, Philadelphia, PA

    Stuart N. Isaacs

Rights and permissions

Reprints and permissions

Copyright information

© 2004 Humana Press Inc., Totowa, NJ

About this protocol

Cite this protocol

Seet, B.T., McFadden, G. (2004). Interaction Analysis of Viral Cytokine-Binding Proteins Using Surface Plasmon Resonance. In: Isaacs, S.N. (eds) Vaccinia Virus and Poxvirology. Methods in Molecular Biology, vol 269. Humana Press. https://doi.org/10.1385/1-59259-789-0:219

Download citation

  • DOI: https://doi.org/10.1385/1-59259-789-0:219

  • Publisher Name: Humana Press

  • Print ISBN: 978-1-58829-229-2

  • Online ISBN: 978-1-59259-789-5

  • eBook Packages: Springer Protocols

Publish with us

Policies and ethics

Search

Navigation