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Potent peptidic fusion inhibitors of influenza virus
Open accessAbstract
Broadly reactive drugs for flu: Drugs for influenza are limited. For those available, viral resistance is rife. Part of the problem is that the virus is constantly mutating. Kadam et al. tested the cell entry stage of the virus life cycle as a drug target (see the Perspective by Whitehead). Cell entry is mediated by the major surface glycoprotein hemagglutinin (HA). This stage can be blocked by broadly neutralizing antibodies binding to HA. The authors generated small cyclic peptides that bind to the same sites on HA as the antibodies and mimic their activity. The peptides are cheap and easy to synthesize, are nontoxic to mice, and prevented infection of cells by many types of influenza virus. Science , this issue p. 496 ; see also p. 450
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“Protein1,5, peptide36 and small-molecule inhibitors37 have been designed to bind to the stem region of group 1 HA and neutralize influenza A viruses, but none recognize the group 2 HA.”
From Design of protein-binding proteins from the target structure alone (2022) · cites this paper as [36]
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Cites
[20] Processing of X-ray diffraction data collected in oscillation mode
Otwinowski, Z., & Minor, W. (1997) · Methods in Enzymology · doi:10.1016/s0076-6879(97)76066-x · Cited by 33,475
Coot : model-building tools for molecular graphics
Emsley, P., & Cowtan, K. (2004) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444904019158 · Cited by 30,571
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
PHENIX : building new software for automated crystallographic structure determination
Adams, P. D., Grosse-Kunstleve, R. W., Hung, L.-W., Ioerger, T. R., McCoy, A. J., Moriarty, N. W., Read, R. J., Sacchettini, J. C., Sauter, N. K., & Terwilliger, T. C. (2002) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444902016657 · Cited by 4,361
Receptor Binding and Membrane Fusion in Virus Entry: The Influenza Hemagglutinin
Skehel, J. J., & Wiley, D. C. (2000) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.69.1.531 · Cited by 2,706
Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 Å resolution
Wilson, I. A., Skehel, J. J., & Wiley, D. C. (1981) · Nature · doi:10.1038/289366a0 · Cited by 2,537
Self-citationAnalytical molecular surface calculation
Connolly, M. L. (1983) · Journal of Applied Crystallography · doi:10.1107/s0021889883010985 · Cited by 2,521
The Future of Peptide‐based Drugs
Craik, D. J., Fairlie, D. P., Liras, S. I., & Price, D. A. (2012) · Chemical Biology & Drug Design · doi:10.1111/cbdd.12055 · Cited by 2,034
Likelihood-enhanced fast translation functions
McCoy, A. J., Grosse‐Kunstleve, R. W., Storoni, L. C., & Read, R. J. (2005) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444905001617 · Cited by 1,641
Structure of influenza haemagglutinin at the pH of membrane fusion
Bullough, P. A., Hughson, F. M., Skehel, J. J., & Wiley, D. C. (1994) · Nature · doi:10.1038/371037a0 · Cited by 1,564
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
Self-citationCorti, D., Voss, J., Gamblin, S. J., Codoni, G., Macagno, A., Jarrossay, D., Vachieri, S. G., Pinna, D., Minola, A., Vanzetta, F., et al. (2011) · Science · doi:10.1126/science.1205669 · Cited by 1,203
Sui, J., Hwang, W. C., Perez, S., Ge, W., Aird, D. R., Chen, L., Santelli, E., Stec, B., Cadwell, G., Ali, M., et al. (2009) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1566 · Cited by 1,128
Highly Conserved Protective Epitopes on Influenza B Viruses
Dreyfus, C., Laursen, N. S., Kwaks, T., Zuijdgeest, D., Khayat, R., Ekiert, D. C., Lee, J. H., Metlagel, Z., Bujny, M. V., Jongeneelen, M. A. C., et al. (2012) · Science · doi:10.1126/science.1222908 · Cited by 857
Self-citationAntiviral agents active against influenza A viruses
Clercq, E. D. (2006) · Nature Reviews Drug Discovery · doi:10.1038/nrd2175 · Cited by 677
Computational Design of Proteins Targeting the Conserved Stem Region of Influenza Hemagglutinin
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
Self-citationTon-That, H., Liu, G., Mazmanian, S. K., Faull, K. F., & Schneewind, O. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.22.12424 · Cited by 567
Cross-neutralization of influenza A viruses mediated by a single antibody loop
Ekiert, D. C., Kashyap, A. K., Steel, J., Rubrum, A. M., Bhabha, G., Khayat, R., Lee, J. H., Dillon, M. A., O’Neil, R. E., Faynboym, A. M., et al. (2012) · Nature · doi:10.1038/nature11414 · Cited by 488
Self-citationStructure of the Uncleaved Human H1 Hemagglutinin from the Extinct 1918 Influenza Virus
Stevens, J., Corper, A. L., Basler, C. F., Taubenberger, J. K., Palese, P., & Wilson, I. A. (2004) · Science · doi:10.1126/science.1093373 · Cited by 477
Self-citationGlobal Transmission of Oseltamivir-Resistant Influenza
Moscona, A. (2009) · New England Journal of Medicine · doi:10.1056/nejmp0900648 · Cited by 471
Structural basis of influenza virus fusion inhibition by the antiviral drug Arbidol
Kadam, R. U., & Wilson, I. A. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1617020114 · Cited by 443
Self-citationWhitehead, T. A., Chevalier, A. A., Song, Y., Dreyfus, C., Fleishman, S. J., de Mattos, C., Myers, C., Kamisetty, H., Blair, P. J., Wilson, I. A., et al. (2012) · Nature Biotechnology · doi:10.1038/nbt.2214 · Cited by 367
Self-citationStructures of influenza A proteins and insights into antiviral drug targets
Das, K., Aramini, J. M., Ma, L.-C., Krug, R. M., & Arnold, E. (2010) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1779 · Cited by 330
Cl–π interactions in protein–ligand complexes
Imai, Y. N., Inoue, Y., Nakanishi, I., & Kitaura, K. (2008) · Protein Science · doi:10.1110/ps.033910.107 · Cited by 218
Russell, R. J., Gamblin, S. J., Haire, L. F., Stevens, D. J., Xiao, B., Ha, Y., & Skehel, J. J. (2004) · Virology · doi:10.1016/j.virol.2004.04.040 · Cited by 180
Nakamura, G. R., Chai, N., Park, S., Chiang, N., Lin, Z., Chiu, H. H., Fong, R., Yan, D., Kim, J., Zhang, J., et al. (2013) · Cell Host & Microbe · doi:10.1016/j.chom.2013.06.004 · Cited by 179
Mechanisms of Hemagglutinin Targeted Influenza Virus Neutralization
Brandenburg, B., Koudstaal, W., Goudsmit, J., Klaren, V., Tang, C., Bujny, M. V., Korse, H. J. W. M., Kwaks, T., Otterstrom, J., Juraszek, J., et al. (2013) · PLoS ONE · doi:10.1371/journal.pone.0080034 · Cited by 173
Self-citationDual Resistance to Adamantanes and Oseltamivir Among Seasonal Influenza A(H1N1) Viruses: 2008–2010
Sheu, T. G., Fry, A. M., Garten, R. J., Deyde, V., Shwe, T., Bullion, L., Peebles, P. J., Li, Y., Klimov, A. I., & Gubareva, L. V. (2010) · The Journal of Infectious Diseases · doi:10.1093/infdis/jiq005 · Cited by 128
Williams, W. V., Kieber‐Emmons, T., VonFeldt, J. M., Greene, M. I., & Weiner, D. B. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)67772-0 · Cited by 109
Structural insights into key sites of vulnerability on HIV ‐1 Env and influenza HA
Julien, J., Lee, P. S., & Wilson, I. A. (2012) · Immunological Reviews · doi:10.1111/imr.12005 · Cited by 97
Self-citationStructural Characterization of Viral Epitopes Recognized by Broadly Cross-Reactive Antibodies
Lee, P. S., & Wilson, I. A. (2014) · Current topics in microbiology and immunology · doi:10.1007/82_2014_413 · Cited by 95
Self-citationLevi, M., Sällberg, M., Rudén, U., Herlyn, D., Maruyama, H., Wigzell, H., Marks, J. D., & Wahrén, B. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.10.4374 · Cited by 83
Kashyap, A. K., Steel, J., Rubrum, A. M., Estellés, A., Briante, R., Ilyushina, N. A., Li, X., Swale, R. E., Faynboym, A. M., Foreman, P. K., et al. (2010) · PLoS Pathogens · doi:10.1371/journal.ppat.1000990 · Cited by 72
Sparrow, E. G., Friede, M., Sheikh, M., Torvaldsen, S., & Newall, A. T. (2016) · Vaccine · doi:10.1016/j.vaccine.2016.08.057 · Cited by 68
Wyrzucki, A., Dreyfus, C., Kohler, I., Steck, M., Wilson, I. A., & Hangartner, L. (2014) · Journal of Virology · doi:10.1128/jvi.00178-14 · Cited by 66
Self-citationKoday, M. T., Nelson, J., Chevalier, A. A., Koday, M., Kalinoski, H. M., Stewart, L. J., Carter, L. P., Nieusma, T., Lee, P. S., Ward, A. B., et al. (2016) · PLoS Pathogens · doi:10.1371/journal.ppat.1005409 · Cited by 55
Self-citationA peptide mimetic of an anti-CD4 monoclonal antibody by rational design
Casset, F., Roux‐Dalvai, F., Mouchet, P., Bès, C., Chardès, T., Granier, C., Mani, J. C., Pugnière, M., Laune, D., Pau, B., et al. (2003) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(03)01131-8 · Cited by 35
Site-Specific Labeling of Proteins via Sortase: Protocols for the Molecular Biologist
Popp, M. W. (2014) · Methods in molecular biology · doi:10.1007/978-1-4939-2272-7_13 · Cited by 12
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Metadata
- Authors
- Kadam, R. U., Juraszek, J., Brandenburg, B., Buyck, C., Schepens, W. B. G., Kesteleyn, B., Stoops, B., Vreeken, R. J., Vermond, J., Goutier, W., Tang, C., Vogels, R., Friesen, R. H. E., Goudsmit, J., van Dongen, M. J. P., & Wilson, I. A.
- Affiliations
- Scripps Research Institute (US)
- Janssen (Netherlands) (NL)
- Janssen (Belgium) (BE)
- Harvard University (US)
- Janssen Prevention Center, Leiden, Netherlands.
- Corresponding author
- Kadam, Rameshwar U.
- Juraszek, Jarek
- Wilson, Ian A.
- ORCID
- Venue
- Science
- Published
- 2017-10-27
- Volume
- 358
- Issue
- 6362
- Pages
- 496-502
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- PMC
- PMC5659926
- OpenAlex
- W2759132244
- Cited by
- 165
- References
- 39
- Citations by year
- 2026: 7 · 2025: 13 · 2024: 16 · 2023: 19 · 2022: 19 · 2021: 16 · 2020: 29 · 2019: 19 · 2018: 24 · 2017: 2
- FWCI
- 16.50
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Science (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institutes of Health (award304792, 1R56 AI117675, award348894, R56 AI127371)
- Topics
- Health Sciences › Medicine › Epidemiology › Influenza Virus Research Studies
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › vaccines and immunoinformatics approaches
- Physical Sciences › Chemistry › Organic Chemistry › Carbohydrate Chemistry and Synthesis
- Keywords
- influenza virus, hemagglutinin, peptide inhibitors, fusion inhibitors, broadly neutralizing antibodies, hypervariable region, membrane fusion, 2009 H1N1 pandemic, antiviral agents
- MeSH terms
- Animals, Antiviral Agents, Humans, Male, Mice, Inbred BALB C, Peptides, Cyclic, Protein Conformation, Drug Design, Crystallography, X-Ray, Complementarity Determining Regions, Mice, Influenza A Virus, H1N1 Subtype, Influenza A Virus, H5N1 Subtype, Virus Internalization, Antibodies, Neutralizing
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