Letter | Published:

Neutralizing antibody to human rhinovirus 14 penetrates the receptor-binding canyon

Nature volume 383, pages 350354 (26 September 1996) | Download Citation

Subjects

Abstract

THE three-dimensional structure of intact human rhinovirus 14 (HRV-14) complexed with Fab fragments (Fabl7-IA) from a strongly neutralizing antibody that binds bivalently to the virion1,2 has been determined to 4.0 Å resolution by a combination of X-ray crystallography and cryo-electron microscopy. In contradiction to the most commonly held model of antibody-mediated neutralization, Fab17-IA does not induce a conformational change in the HRV-14 capsid. Instead, the paratope of the antibody undergoes a large conformational change to accommodate the epitope. Unlike any previously described antibody–antigen structure, the conserved framework region of the antibody makes extensive contact with the viral surface. Fabl7-IA penetrates deep within the canyon in which the cellular receptor for HRV-14 binds3,4. Hence, it is unlikely that viral quaternary structure evolves merely to evade immune recognition. Instead, the shape and position of the receptor-binding region on a virus probably dictates receptor binding and subsequent uncoating events and has little or no influence on concealing the virus from the immune system.

Access optionsAccess options

Rent or Buy article

Get time limited or full article access on ReadCube.

from$8.99

All prices are NET prices.

References

  1. 1.

    , & in Molecular Aspects of Picornavirus Infection and Detection (eds Semler, B. L & Ehrenfeld, E.) 155–167 (Am. Soc. Microbiol., Washington, DC, 1989).

  2. 2.

    , , , & Proc. Natl Acad. Sci. USA 90, 7015–7018 (1993).

  3. 3.

    et al. Nature 317, 145–153 (1985).

  4. 4.

    et al. Proc. Natl Acad. Sci. USA 90, 507–511 (1993).

  5. 5.

    et al. J. Virol. 67, 1148–1158 (1993).

  6. 6.

    , , , & (US Department of Health and Human Services, Public Health Service, NIH, Bethesda, MD, 1987).

  7. 7.

    et al. J. Mol. Biol. 256, 813–817 (1996).

  8. 8.

    & Trends Biotechnol. 12, 275–279 (1994).

  9. 9.

    et al. Science 233, 1286–1293 (1986).

  10. 10.

    et al. Structure 1, 51–68 (1993).

  11. 11.

    J. Biol. Chem. 264, 14587–14590 (1989).

  12. 12.

    , , & J. Virol 63, 36–42 (1989).

  13. 13.

    thesis, Univ. Wisconsin, USA (1991).

  14. 14.

    et al. Nature Struct. Biol. 2, 232–243 (1995).

  15. 15.

    et al. J. Virol. 66, 1835–1840 (1992).

  16. 16.

    et al. Nature 327, 709–716 (1989).

  17. 17.

    et al. EMBO J 14, 1690–1696 (1995).

  18. 18.

    , , & Virology 181, 694–702 (1991).

  19. 19.

    et al. Proc. Natl Acad. Sci. USA 92, 10648–10652 (1995).

  20. 20.

    , , , & Virology 214, 559–570 (1995).

  21. 21.

    et al. Nature 376, 92–94 (1995).

  22. 22.

    & J. Virol. 67, 390–397 (1993).

  23. 23.

    et al. J. Mol. Biol 177, 417–430 (1984).

  24. 24.

    in Data Collection and Processing (eds Sawyer, L., Isaacs, N. & Bailey, S.) 56–62 (SERC Daresbury Laboratory, Warrington, UK, 1993).

  25. 25.

    & Acta Crystallogr. A46, 783–792 (1990).

  26. 26.

    et al. J. Mol. Biol. 240, 127–137 (1994).

  27. 27.

    et al. J. Appl. Cryst. 25, 166–180 (1992).

  28. 28.

    X-plor (Version 3.1) User's Guide (Yale Univ., New Haven, CT, 1992).

  29. 29.

    Immunomethods 3, 191–196 (1993).

  30. 30.

    et al. Science 235, 182–191 (1987).

Download references

Author information

Affiliations

  1. Department of Biological Sciences, Purdue University, West Lafayette, Indiana 47907-1392, USA

    • Thomas J. Smith
    • , Elaine S. Chase
    • , Timothy J. Schmidt
    • , Norman H. Olson
    •  & Timothy S. Baker

Authors

  1. Search for Thomas J. Smith in:

  2. Search for Elaine S. Chase in:

  3. Search for Timothy J. Schmidt in:

  4. Search for Norman H. Olson in:

  5. Search for Timothy S. Baker in:

About this article

Publication history

Received

Accepted

Published

DOI

https://doi.org/10.1038/383350a0

Further reading

Comments

By submitting a comment you agree to abide by our Terms and Community Guidelines. If you find something abusive or that does not comply with our terms or guidelines please flag it as inappropriate.