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Peer-reviewedCC BY 4.0ACS Omega

Potent Antivirals for Respiratory Syncytial Virus Detected via Peptide-Based Fusion Inhibitor Screening

  • Satoshi Suzuki1,2
  • Yusuke Usui3,4
  • Keisuke Aoki3,4
  • Haruto Amano3
  • Yoshiki Hiramatsu1
  • Akie Nishiyama1
  • Koichi Hashimoto5
  • Kazutaka Murayama6
  • Hironori Hayashi6
  • Stefan G. Sarafianos7
  • Shinya Oishi3,4
  • Eiichi N. Kodama1,6
7 affiliations
  1. 1Tohoku University Graduate School of Medicine , , 2-1 Seiryo-machi , Aoba-ku, , ,
  2. 2Japan Institute for Health Security , , , ,
  3. 3Kyoto Pharmaceutical University , , 1 Misasagi-Shichono-cho , Yamashina-ku, ,
  4. 4Kyoto University , , 46-29 Yoshida-Shimo-Adachi-cho , Sakyo-ku, ,
  5. 5Fukushima Medical University , , 1 Hikariga-oka , , ,
  6. 6Tohoku University , , 2-1 Seiryo-machi , Aoba-ku, , ,
  7. 7Emory University School of Medicine , , , ,
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Abstract

The respiratory syncytial virus (RSV) causes fatal pneumonia in neonates, infants, and older adults. However, no approved antiviral drugs exist for RSV; furthermore, the currently available antibody-based therapies are expensive and do not provide complete protection against RSV infections. Thus, developing anti-RSV agents for treating RSV infections is crucial. We previously established a rational strategy for designing peptide-based fusion inhibitors targeting class I fusion proteins, which are essential for the membrane fusion of viruses and host cells. Here, we used this strategy to identify peptide-based fusion inhibitors that block the interaction between the heptad repeat 1 and 2 (HR1 and -2) regions of the RSV F protein and identified four key amino acid regions involved in the HR1–HR2 interaction. Peptides, including the key amino acid regions VirRS2 and VirRS8, inhibited the replication of the RSV-A2 strain. We confirmed the structure–activity relationships using crystal structure coordinates and AlphaFold2-based structural predictions. These results may advance novel RSV fusion inhibitor development.

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Cite

BibTeXRIS
BibTeX
@article{suzuki2026potent,
  title = {{Potent Antivirals for Respiratory Syncytial Virus Detected via Peptide-Based Fusion Inhibitor Screening}},
  author = {Satoshi Suzuki and Yusuke Usui and Keisuke Aoki and Haruto Amano and Yoshiki Hiramatsu and Akie Nishiyama and Koichi Hashimoto and Kazutaka Murayama and Hironori Hayashi and Stefan G. Sarafianos and Shinya Oishi and Eiichi N. Kodama},
  journal = {ACS Omega},
  year = {2026},
  month = oct,
  doi = {10.1021/acsomega.6c05253},
  url = {https://pubs.acs.org/acsodf/article/11/41/63006/5446588/Potent-Antivirals-for-Respiratory-Syncytial-Virus},
  note = {CC BY 4.0},
}
RIS
TY  - JOUR
TI  - Potent Antivirals for Respiratory Syncytial Virus Detected via Peptide-Based Fusion Inhibitor Screening
AU  - Satoshi Suzuki
AU  - Yusuke Usui
AU  - Keisuke Aoki
AU  - Haruto Amano
AU  - Yoshiki Hiramatsu
AU  - Akie Nishiyama
AU  - Koichi Hashimoto
AU  - Kazutaka Murayama
AU  - Hironori Hayashi
AU  - Stefan G. Sarafianos
AU  - Shinya Oishi
AU  - Eiichi N. Kodama
PY  - 2026
DA  - 2026/10/07
JO  - ACS Omega
DO  - 10.1021/acsomega.6c05253
UR  - https://pubs.acs.org/acsodf/article/11/41/63006/5446588/Potent-Antivirals-for-Respiratory-Syncytial-Virus
AB  - The respiratory syncytial virus (RSV) causes fatal pneumonia in neonates, infants, and older adults. However, no approved antiviral drugs exist for RSV; furthermore, the currently available antibody-based therapies are expensive and do not provide complete protection against RSV infections. Thus, developing anti-RSV agents for treating RSV infections is crucial. We previously established a rational strategy for designing peptide-based fusion inhibitors targeting class I fusion proteins, which are essential for the membrane fusion of viruses and host cells. Here, we used this strategy to identify peptide-based fusion inhibitors that block the interaction between the heptad repeat 1 and 2 (HR1 and -2) regions of the RSV F protein and identified four key amino acid regions involved in the HR1–HR2 interaction. Peptides, including the key amino acid regions VirRS2 and VirRS8, inhibited the replication of the RSV-A2 strain. We confirmed the structure–activity relationships using crystal structure coordinates and AlphaFold2-based structural predictions. These results may advance novel RSV fusion inhibitor development.
SN  - 2470-1343
ER  -