Cited by 170Influenza Virus Research Studiesvaccines and immunoinformatics approachesCarbohydrate Chemistry and Synthesis

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Potent peptidic fusion inhibitors of influenza virus

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Kadam, Rameshwar U., Juraszek, Jarek, Brandenburg, Boerries, Buyck, Christophe, Schepens, Wim B. G., Kesteleyn, Bart, Stoops, Bart, Vreeken, Rob J., Vermond, Jan, Goutier, Wouter, Tang, Chan, Vogels, Ronald, Friesen, Robert H. E., Goudsmit, Jaap, van Dongen, Maria J. P., Wilson, Ian A.·2017·Science

DOI 10.1126/science.aan0516PMC PMC5659926

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Abstract

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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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: Kadam, Rameshwar U.
Juraszek, Jarek
Brandenburg, Boerries
Buyck, Christophe
Schepens, Wim B. G.
Kesteleyn, Bart
Stoops, Bart
Vreeken, Rob J.
Vermond, Jan
Goutier, Wouter
Tang, Chan
Vogels, Ronald
van Dongen, Maria J. P.
Wilson, Ian A.
Venue: Science
Publisher: American Association for the Advancement of Science (AAAS)
Published: 2017-10-27
Volume: 358
Issue: 6362
Pages: 496-502
ISSN: 0036-8075 (ISSN-L)
1095-9203
DOI: 10.1126/science.aan0516
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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Potent peptidic fusion inhibitors of influenza virus

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