1. A Broad-Spectrum Antiviral Peptide Blocks Infection of Viruses by Binding to Phosphatidylserine in the Viral Envelope
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Luteijn, Rutger D., Praest, Patrique, Thiele, Frank, Sadasivam, Saravanan Manikam, Singethan, Katrin, Drijfhout, Jan W., Bach, Christian, de Boer, Steffen Matthijn, Lebbink, Robert J., Tao, Sha, Helfer, Markus, Bach, Nina C., Protzer, Ulrike, Costa, Ana I., Killian, J. Antoinette, Drexler, Ingo, Wiertz, Emmanuel J.H.J., Virologie, Sub Membrane Biochemistry & Biophysics, LS Virologie, Membrane Biochemistry and Biophysics, Virologie, Sub Membrane Biochemistry & Biophysics, LS Virologie, and Membrane Biochemistry and Biophysics
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0301 basic medicine ,medicine.drug_class ,viruses ,Phospholipid ,membrane phosphatidylserine ,Peptide ,Phosphatidylserines ,medicine.disease_cause ,Antiviral Agents ,Article ,Virus ,03 medical and health sciences ,chemistry.chemical_compound ,0302 clinical medicine ,Viral envelope ,medicine ,Humans ,lcsh:QH301-705.5 ,chemistry.chemical_classification ,Hepatitis B virus ,Cowpox virus ,envelope disruption ,General Medicine ,Phosphatidylserine ,Virology ,3. Good health ,030104 developmental biology ,enveloped viruses ,chemistry ,antiviral peptide ,lcsh:Biology (General) ,Viral Envelope ,Antiviral Peptide ,Enveloped Viruses ,Membrane Phosphatidylserine ,Envelope Disruption ,Antiviral drug ,Peptides ,030215 immunology - Abstract
The ongoing threat of viral infections and the emergence of antiviral drug resistance warrants a ceaseless search for new antiviral compounds. Broadly-inhibiting compounds that act on elements shared by many viruses are promising antiviral candidates. Here, we identify a peptide derived from the cowpox virus protein CPXV012 as a broad-spectrum antiviral peptide. We found that CPXV012 peptide hampers infection by a multitude of clinically and economically important enveloped viruses, including poxviruses, herpes simplex virus-1, hepatitis B virus, HIV-1, and Rift Valley fever virus. Infections with non-enveloped viruses such as Coxsackie B3 virus and adenovirus are not affected. The results furthermore suggest that viral particles are neutralized by direct interactions with CPXV012 peptide and that this cationic peptide may specifically bind to and disrupt membranes composed of the anionic phospholipid phosphatidylserine, an important component of many viral membranes. The combined results strongly suggest that CPXV012 peptide inhibits virus infections by direct interactions with phosphatidylserine in the viral envelope. These results reiterate the potential of cationic peptides as broadly-acting virus inhibitors.
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