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Interaction of Human Respiratory Syncytial Virus (HRSV) Matrix Protein with Resveratrol Shows Antiviral Effect.

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  • Additional Information
    • Source:
      Publisher: MDPI Country of Publication: Switzerland NLM ID: 101092791 Publication Model: Electronic Cited Medium: Internet ISSN: 1422-0067 (Electronic) Linking ISSN: 14220067 NLM ISO Abbreviation: Int J Mol Sci Subsets: MEDLINE
    • Publication Information:
      Original Publication: Basel, Switzerland : MDPI, [2000-
    • Subject Terms:
      Resveratrol*/pharmacology ; Resveratrol*/chemistry ; Respiratory Syncytial Virus, Human*/drug effects ; Respiratory Syncytial Virus, Human*/metabolism ; Antiviral Agents*/pharmacology ; Antiviral Agents*/chemistry ; Viral Matrix Proteins*/metabolism ; Viral Matrix Proteins*/chemistry; Humans ; Protein Binding ; Cell Line, Tumor ; Stilbenes/pharmacology ; Stilbenes/chemistry
    • Abstract:
      The respiratory syncytial virus (RSV) matrix protein plays key roles in the virus life cycle and is essential for budding, as it stimulates the optimal membrane curvature necessary for the emergence of viral particles. Resveratrol, a polyphenol (3,4',5-trihydroxy-trans-stilbene) produced by plants, exhibits pharmacological effects, including anti-inflammatory and antiviral activities. In this study, resveratrol was tested in HEp-2 (Epidermoid carcinoma of the larynx cell) cells for its post-infection effects, and recombinant M protein was produced to characterize the biophysical mechanisms underlying this interaction. The CC50 (Cytotoxic concentration 50%) value for resveratrol was determined to be 297 μM over 48 h, and the results from the HEp-2 cell cultures demonstrated a viral inhibition of 42.7% in the presence of resveratrol, with an EC50 (Half maximal effective concentration) of 44.26 μM. This mechanism may occur through interaction with the M protein responsible for the budding of mature viral particles. Biophysical assays enabled us to characterize the interaction of the M/resveratrol complex as an entropically driven bond, guided by hydrophobic interactions at the dimerization interface of the M protein, which is essential for the stabilization and formation of the oligomers necessary for viral budding. These findings suggest that one of the targets for resveratrol binding is the M protein, indicating a potential site for blocking the progression of the infection.
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    • Grant Information:
      2019/04646-9, 2021/14349-1 Fapesp
    • Contributed Indexing:
      Keywords: M protein; and resveratrol; respiratory syncytial virus
    • Accession Number:
      Q369O8926L (Resveratrol)
      0 (Antiviral Agents)
      0 (Viral Matrix Proteins)
      0 (Stilbenes)
    • Publication Date:
      Date Created: 20241217 Date Completed: 20241217 Latest Revision: 20250104
    • Publication Date:
      20250104
    • Accession Number:
      PMC11640991
    • Accession Number:
      10.3390/ijms252312790
    • Accession Number:
      39684498