The DOI matches its Crossref record; 8 of the 8 references it cites were found in a registry or an index.
Cross-neutralization of influenza A viruses mediated by a single antibody loop
Open accessAbstract
Immune recognition of protein antigens relies on the combined interaction of multiple antibody loops, which provide a fairly large footprint and constrain the size and shape of protein surfaces that can be targeted. Single protein loops can mediate extremely high-affinity binding, but it is unclear whether such a mechanism is available to antibodies. Here we report the isolation and characterization of an antibody called C05, which neutralizes strains from multiple subtypes of influenza A virus, including H1, H2 and H3. X-ray and electron microscopy structures show that C05 recognizes conserved elements of the receptor-binding site on the haemagglutinin surface glycoprotein. Recognition of the haemagglutinin receptor-binding site is dominated by a single heavy-chain complementarity-determining region 3 loop, with minor contacts from heavy-chain complementarity-determining region 1, and is sufficient to achieve nanomolar binding with a minimal footprint. Thus, binding predominantly with a single loop can allow antibodies to target small, conserved functional sites on otherwise hypervariable antigens.
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PHENIX : a comprehensive Python-based system for macromolecular structure solution
Adams, P. D., Afonine, P. V., Bunkóczi, G., Chen, V. B., Davis, I. W., Echols, N., Headd, J. J., Hung, L.-W., Kapral, G. J., Grosse-Kunstleve, R. W., et al. (2010) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444909052925 · Cited by 23,716
Phaser crystallographic software
McCoy, A. J., Grosse-Kunstleve, R. W., Adams, P. D., Winn, M. D., Storoni, L. C., & Read, R. J. (2007) · Journal of Applied Crystallography · doi:10.1107/s0021889807021206 · Cited by 20,612
MolProbity : all-atom structure validation for macromolecular crystallography
Chen, V. B., Arendall, W. B., Headd, J. J., Keedy, D. A., Immormino, R. M., Kapral, G. J., Murray, L. W., Richardson, J. S., & Richardson, D. C. (2010) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444909042073 · Cited by 14,115
Antibody Recognition of a Highly Conserved Influenza Virus Epitope
Ekiert, D. C., Bhabha, G., Elsliger, M.-A., Friesen, R. H. E., Jongeneelen, M., Throsby, M., Goudsmit, J., & Wilson, I. A. (2009) · Science · doi:10.1126/science.1171491 · Cited by 1,326
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Structure of HIV-1 gp120 V1/V2 domain with broadly neutralizing antibody PG9
McLellan, J. S., Pancera, M., Carrico, C., Gorman, J., Julien, J.-P., Khayat, R., Louder, R., Pejchal, R., Sastry, M., Dai, K., et al. (2011) · Nature · doi:10.1038/nature10696 · Cited by 830
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Pejchal, R., Doores, K. J., Walker, L. M., Khayat, R., Huang, P.-S., Wang, S.-K., Stanfield, R. L., Julien, J.-P., Ramos, A., Crispin, M., et al. (2011) · Science · doi:10.1126/science.1213256 · Cited by 694
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Fleishman, S. J., Whitehead, T. A., Ekiert, D. C., Dreyfus, C., Corn, J. E., Strauch, E.-M., Wilson, I. A., & Baker, D. (2011) · Science · doi:10.1126/science.1202617 · Cited by 585
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Cao, L., Coventry, B., Goreshnik, I., Huang, B., Sheffler, W., Park, J. S., Jude, K. M., Marković, I., Kadam, R. U., Verschueren, K. H. G., et al. (2022) · Nature · doi:10.1038/s41586-022-04654-9 · Cited by 577
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Xu, S., Yang, K., Li, R., & Zhang, L. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21186582 · Cited by 368
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Kadam, R. U., Juraszek, J., Brandenburg, B., Buyck, C., Schepens, W. B. G., Kesteleyn, B., Stoops, B., Vreeken, R. J., Vermond, J., Goutier, W., et al. (2017) · Science · doi:10.1126/science.aan0516 · Cited by 165
Self-citationStrauch, E.-M., Bernard, S. M., La, D., Bohn, A. J., Lee, P. S., Anderson, C. E., Nieusma, T., Holstein, C. A., Garcia, N. K., Hooper, K. A., et al. (2017) · Nature Biotechnology · doi:10.1038/nbt.3907 · Cited by 119
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Metadata
- Authors
- Ekiert, D. C., Kashyap, A. K., Steel, J., Rubrum, A., Bhabha, G., Khayat, R., Lee, J. H., Dillon, M. A., O’Neil, R. E., Faynboym, A. M., Horowitz, M., Horowitz, L., Ward, A. B., Palese, P., Webby, R., Lerner, R. A., Bhatt, R. R., & Wilson, I. A.
- Venue
- Nature
- Published
- 2012-09
- Volume
- 489
- Issue
- 7417
- Pages
- 526-532
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- OpenAlex
- W2077219861
- Cited by
- 481
- References
- 8
- FWCI
- 24.77
- Type
- journal article
- Language
- en
- Open access
- green
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- Ekiert, D. C., Kashyap, A. K., Steel, J., Rubrum, A., Bhabha, G., Khayat, R., Lee, J. H., Dillon, M. A., O’Neil, R. E., Faynboym, A. M., Horowitz, M., Horowitz, L., Ward, A. B., Palese, P., Webby, R., Lerner, R. A., Bhatt, R. R., & Wilson, I. A. (2012). Cross-neutralization of influenza A viruses mediated by a single antibody loop. Nature. https://doi.org/10.1038/nature11414
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