Identification of the amino acid residue important for fusion of severe fever with thrombocytopenia syndrome virus glycoprotein

Tani, Hideki; Kawachi, Kengo; Kimura, Miyuki; Taniguchi, Satoshi; Shimojima, Masayuki; Fukushi, Shuetsu; Igarashi, Manabu; Morikawa, Shigeru; Saijo, Masayuki

doi:10.1016/j.virol.2019.06.014

Cited by 13 publications

(9 citation statements)

References 19 publications

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“…Of the variable sites identified in Gc, position 962 is known to be important for glycoprotein-mediated fusion ability. Replacement of Arginine (R) with Serine (S) at this site could induce a more efficient syncytium formation (Tani et al 2019). In this position, all the analyzed strains use S, except the HB29 strain, which uses R (Fig.…”

Section: Discussionmentioning

confidence: 96%

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Novel SFTSV Phylogeny Reveals New Reassortment Events and Migration Routes

Zhang

et al. 2020

Virol. Sin.

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Section: Discussionmentioning

confidence: 96%

“…5B, Supplementary Table S7). HB29 belongs to the C3 genotype and is often being used for in vitro studies, despite it exhibits no or a weak syncytium formation only (Tani et al 2019).…”

Section: Discussionmentioning

confidence: 99%

Novel SFTSV Phylogeny Reveals New Reassortment Events and Migration Routes

Zhang

et al. 2020

Virol. Sin.

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“…In this study, we tried to integrate ions and betasesquiphellandrene by in silico methods and analyze its interaction with Spike protein (Sp) [8] of SARS-CoV2 and membrane glycoprotein polyprotein (MGp) [9] of SFTS virus. Both of these proteins belong to viral domain and have a role in access to human cytological areas, particularly targeting respiratory surfaces.…”

Section: Introductionmentioning

confidence: 99%

Molecular docking and simulation investigation: effect of beta-sesquiphellandrene with ionic integration on SARS-CoV2 and SFTS viruses

Joshi

Kaushik

2020

Journal of Genetic Engineering and Biotechnology

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Background At present, viral diseases become major concern for the world. SARS-CoV2 and SFTS viruses are deadly in nature, and there is a need for developing best treatments for them. Modern in silico approaches were found to be very handy in determining putative drug molecules. In this study, we analyze interaction of beta-sesquiphellandrene (compound belongs to ginger) with spike protein (Sp) and membrane glycoprotein polyprotein (MPp). Results Our molecular docking and simulation study reveals the perfect binding pocket of Sp and MPp holding beta-sesquiphellandrene (bS). Binding energies for MPp-bS and Sp-bS were found to be − 9.5 kcal/mol and − 10.3 kcal/mol respectively. RMSD and RMSF values for docked complexes were found to be in selectable range, i.e., 1 to 3 Å and 1 to 8 Å respectively. Modern computational tools were used here to make this investigation fast and effective. Further, ADME analysis reveals the therapeutic validations for beta-sesquiphellandrene to act as a useful pharmacoactive compound. Beta-sesquiphellandrene provides not only inhibitory effect on spike protein of SARS-CoV2 but also similar inhibitory effects on membrane glycoprotein polyprotein complex of SFTS virus, which hampers the pathological initiation of the diseases caused by both the viruses, i.e., COVID-19 and severe fever with thrombocytopenia syndrome. Conclusion This method of computational analysis was found to be rapid and effective, and opens new doors in the domain of in silico drug discovery. Beta-sesquiphellandrene can be used as effective medicine to control these harmful pathogens after wet lab validations.

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“…In all of the Japanese sequences, this change was to E (Glu), whereas the Korean sequences presented three variations: one E (Glu) (strain 16KS28), two N (Asn) (strain 16KS31 and 16KS40), and one G (Gly) (strain 16KS26). A Japanese research group reported that substitution of the amino acid residue 962 (R > S) is crucial for the membrane fusion step of viral infection [20]. In our data, all of the KNIH strains except for strain 15KS7 (accession no.…”

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confidence: 53%

Genetic diversity and evolutionary history of Korean isolates of severe fever with thrombocytopenia syndrome virus from 2013–2016

et al. 2020

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Severe fever with thrombocytopenia syndrome (SFTS) is caused by SFTS virus (SFTSV). Although SFTS originated in China, it is an emerging infectious disease with prevalence confirmed in Japan, Korea, and Vietnam. The full-length genomes of 51 Korean SFTSV isolates from 2013 to 2016 were sequenced, and the sequences were deposited into a public database (GenBank) and analyzed to elucidate the phylogeny and evolution of the virus. Although most of the Korean SFTSV isolates were closely related to previously reported Japanese isolates, some were closely related to previously reported Chinese isolates. We identified one Korean strain that appears to have resulted from multiple inter-lineage reassortments. Several nucleotide and amino acid variations specific to the Korean isolates were identified. Future studies should focus on how these variations affect virus pathogenicity and evolution.

show abstract

Identification of the amino acid residue important for fusion of severe fever with thrombocytopenia syndrome virus glycoprotein

Cited by 13 publications

References 19 publications

Novel SFTSV Phylogeny Reveals New Reassortment Events and Migration Routes

Novel SFTSV Phylogeny Reveals New Reassortment Events and Migration Routes

Molecular docking and simulation investigation: effect of beta-sesquiphellandrene with ionic integration on SARS-CoV2 and SFTS viruses

Genetic diversity and evolutionary history of Korean isolates of severe fever with thrombocytopenia syndrome virus from 2013–2016

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