Monomeric catechin and dimeric procyanidin B2 against human norovirus surrogates and their physicochemical interactions
| Autor: | Dan Liu, Pengbo Liu, Haixia Yang, Jianjun Deng, Snehal S. Joshi, Doris H. D'Souza, Yan Yu, Daidi Fan, Ruijuan Zhang, Chao Zhang |
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| Rok vydání: | 2018 |
| Předmět: |
0301 basic medicine
Interaction viruses 030106 microbiology ved/biology.organism_classification_rank.species Virus Attachment Viral Plaque Assay medicine.disease_cause Antiviral Agents Procyanidin B2 Microbiology Catechin Article Foodborne Diseases 03 medical and health sciences chemistry.chemical_compound P domain medicine Animals Biflavonoids Humans Proanthocyanidins Infectivity Feline calicivirus biology ved/biology Norovirus virus diseases biochemical phenomena metabolism and nutrition biology.organism_classification 030104 developmental biology chemistry Capsid Biochemistry Polyphenol Cats Virus Inactivation Calicivirus Feline Food Science Murine norovirus |
| Zdroj: | Food Microbiology |
| ISSN: | 0740-0020 |
| Popis: | Plant polyphenols have shown antiviral activity against several human pathogens, but their physicochemical interactions are not well-understood. The objectives of this study were to compare the antiviral activity between monomeric catechin and dimeric procyanidin B2 (PB2) using cultivable human norovirus surrogates (feline calicivirus (FCV-F9) and murine norovirus (MNV-1)) and to understand their potential antiviral mechanism using virus-like particles (VLPs) and the P domain of human norovirus GII (HNoV GII.4). Surrogate viruses at 5 log PFU/mL were treated with 0.5–5 mg/mL monomeric catechin monohydrate, PB2 or phosphate buffered saline (PBS, pH 7.2; control) at 37 °C over 24 h. Infectivity was determined using plaque assays and data from triplicate experiments were statistically analyzed. PB2 at 0.5 mg/mL and 1 mg/mL reduced FCV-F9 to undetectable levels after 3 h and MNV-1 by 0.21 and 1.23 log PFU after 24 h, respectively. Monomeric catechins at 1 mg/mL reduced FCV-F9 to undetectable levels after 6 h and MNV-1 titers to undetectable levels after 24 h. In addition, PB2 was shown to directly bind the P domain, the main capsid structure of HNoVs in the ratio of 1:1 through spontaneous interactions. Electrostatic interactions played a dominant role between PB2 and the P domain. PB2 significantly altered tertiary but not secondary structures of VLPs. Transmission electron microscopy demonstrated that PB2 aggregated VLPs, further indicating interactions between them. These findings indicate that PB2 causes structural changes of the P domain of VLPs, mainly through direct interaction leading to HNoV inactivation. Highlights • Polymeric procyanidins cause higher reduction of human norovirus surrogate titers than monomers. • Binding of procyanidin to human norovirus-like particles alters capsid structure. • Procyanidin binding to viral capsid results in decreased infectivity. |
| Databáze: | OpenAIRE |
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