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https://doi.org/10.1371/journal.pone.0054761
Title: | Interaction Domain of Glycoproteins gB and gH of Marek's Disease Virus and Identification of an Antiviral Peptide with Dual Functions | Authors: | Chi X.-J. Lu Y.-X. Zhao P. Li C.-G. Wang X.-J. Wang M. |
Keywords: | glutamic acid glycoprotein glycoprotein gB glycoprotein gH lysine unclassified drug antivirus agent glycoprotein B, Marek's disease virus glycoprotein H, Marek's disease virus peptide protein binding virus antigen virus envelope protein animal cell article circular dichroism controlled study embryo gel filtration Marek disease nonhuman prediction protein binding protein conformation protein determination protein domain protein function protein protein interaction tandem repeat virus cell interaction wild type amino acid sequence animal chemistry chick embryo fibroblast Mardivirus metabolism molecular genetics protein secondary structure protein tertiary structure virology Amino Acid Sequence Animals Antigens, Viral Antiviral Agents Chick Embryo Fibroblasts Herpesvirus 2, Gallid Molecular Sequence Data Peptides Protein Binding Protein Interaction Domains and Motifs Protein Structure, Secondary Protein Structure, Tertiary Viral Envelope Proteins |
Issue Date: | 2013 | Citation: | Chi X.-J., Lu Y.-X., Zhao P., Li C.-G., Wang X.-J., Wang M. (2013). Interaction Domain of Glycoproteins gB and gH of Marek's Disease Virus and Identification of an Antiviral Peptide with Dual Functions. PLoS ONE 8 (2) : e54761. ScholarBank@NUS Repository. https://doi.org/10.1371/journal.pone.0054761 | Rights: | Attribution 4.0 International | Abstract: | Our previous study reported that both glycoproteins gB and gH of the herpesvirus Marek's disease virus (MDV) contain eleven potential heptad repeat domains. These domains overlap with ?-helix-enriched hydrophobic regions, including the gH-derived HR1 (gHH1) and HR3 (gHH3) and gB-derived HR1 (gBH1) regions, which demonstrate effective antiviral activity, with 50% inhibitory concentrations (IC50) of less than 12 ?M. Plaque formation and chicken embryo infection assays confirmed these results. In this study, biochemical and biophysical analyses detected potential interactions between these peptides. gHH1, gHH3, and gBH1 were found to interact with each other in pairs. The complex formed by gHH3 and gBH1 showed the most stable interaction at a molar ratio of 1:3, the binding between gHH1 and gBH1 was relatively weak, and no interaction was observed between the three HR peptides. These results indicate that gHH3 and gBH1 are likely the key contributors to the interaction between gB and gH. Furthermore, each HR peptide from herpesvirus glycoproteins did not effectively inhibit virus infection compared with peptides from a class I enveloped virus. In this report, the HR mimic peptide modified with a double glutamic acid (EE) or a double lysine (KK) at the non-interactive sites (i.e., solvent-accessible sites) did not noticeably affect the antiviral activity compared with the wild-type HR peptide, whereas tandem peptides from gH-derived gHH1 and gB-derived gBH1 (i.e., gBH1-Linker-gHH1) produced efficient antiviral effects, unlike the individual peptides. The proposed interpretation of inhibition of entry has been addressed. Our results support the hypothesis that the interaction domain between glycoproteins gH and gB is a critical target in the design of inhibitors of herpesvirus infection. © 2013 Chi et al. | Source Title: | PLoS ONE | URI: | https://scholarbank.nus.edu.sg/handle/10635/161343 | ISSN: | 19326203 | DOI: | 10.1371/journal.pone.0054761 | Rights: | Attribution 4.0 International |
Appears in Collections: | Elements Staff Publications |
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