6M56

Solution NMR Structure of Peptide P9R

Summary for 6M56

• Entry DOI: 10.2210/pdb6m56/pdb
• NMR Information: BMRB: 36321
• Descriptor: Peptide P9R (1 entity in total)
• Functional Keywords: antiviral protein
• Biological source: Mus musculus (Mouse)
• Total number of polymer chains: 1
• Total formula weight: 3418.08

Authors

Yuen, K.Y.,Zhao, H.J.,Yung, T.M.,Sze, K.H. (deposition date: 2020-03-10, release date: 2020-09-09, Last modification date: 2024-05-01)

Primary citation

Zhao, H.,To, K.K.W.,Sze, K.H.,Yung, T.T.,Bian, M.,Lam, H.,Yeung, M.L.,Li, C.,Chu, H.,Yuen, K.Y.
A broad-spectrum virus- and host-targeting peptide against respiratory viruses including influenza virus and SARS-CoV-2.
Nat Commun, 11:4252-4252, 2020

PubMed Abstract: The 2019 novel respiratory virus (SARS-CoV-2) causes COVID-19 with rapid global socioeconomic disruptions and disease burden to healthcare. The COVID-19 and previous emerging virus outbreaks highlight the urgent need for broad-spectrum antivirals. Here, we show that a defensin-like peptide P9R exhibited potent antiviral activity against pH-dependent viruses that require endosomal acidification for virus infection, including the enveloped pandemic A(H1N1)pdm09 virus, avian influenza A(H7N9) virus, coronaviruses (SARS-CoV-2, MERS-CoV and SARS-CoV), and the non-enveloped rhinovirus. P9R can significantly protect mice from lethal challenge by A(H1N1)pdm09 virus and shows low possibility to cause drug-resistant virus. Mechanistic studies indicate that the antiviral activity of P9R depends on the direct binding to viruses and the inhibition of virus-host endosomal acidification, which provides a proof of concept that virus-binding alkaline peptides can broadly inhibit pH-dependent viruses. These results suggest that the dual-functional virus- and host-targeting P9R can be a promising candidate for combating pH-dependent respiratory viruses.

PubMed: 32843628
DOI: 10.1038/s41467-020-17986-9

Experimental method

SOLUTION NMR