RETRACTED: Antiviral and myocyte protective effects of IL-28A in coxsackievirus B3-induced myocarditis

Wang, Shihong; Huang, Xingyuan; Zhang, Jing; Huang, Congxin

doi:10.1016/j.bjid.2014.10.007

Cited by 3 publications

(2 citation statements)

References 47 publications

(39 reference statements)

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“…The pathogenesis of CVB infection is believed to be the consequence of cellular damage or death due to virus replication [ 1 , 6 ]. In addition, the inflammatory and immune response induced by CVB infection also plays an important role in viral myocarditis [ 9 , 10 , 11 , 12 , 13 ]. In spite of the extensive investigations, the pathogenesis of CVB infection has not been fully understood.…”

Section: Introductionmentioning

confidence: 99%

Protein 2B of Coxsackievirus B3 Induces Autophagy Relying on Its Transmembrane Hydrophobic Sequences

Zhai

Chen

et al. 2016

Viruses

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Coxsackievirus B (CVB) belongs to Enterovirus genus within the Picornaviridae family, and it is one of the most common causative pathogens of viral myocarditis in young adults. The pathogenesis of myocarditis caused by CVB has not been completely elucidated. In CVB infection, autophagy is manipulated to facilitate viral replication. Here we report that protein 2B, one of the non-structural proteins of CVB3, possesses autophagy-inducing capability. The autophagy-inducing motif of protein 2B was identified by the generation of truncated 2B and site-directed mutagenesis. The expression of 2B alone was sufficient to induce the formation of autophagosomes in HeLa cells, while truncated 2B containing the two hydrophobic regions of the protein also induced autophagy. In addition, we demonstrated that a single amino acid substitution (56V→A) in the stem loop in between the two hydrophobic regions of protein 2B abolished the formation of autophagosomes. Moreover, we found that 2B and truncated 2B with autophagy-inducting capability were co-localized with LC3-II. This study indicates that protein 2B relies on its transmembrane hydrophobic regions to induce the formation of autophagosomes, while 56 valine residue in the stem loop of protein 2B might exert critical structural influence on its two hydrophobic regions. These results may provide new insight for understanding the molecular mechanism of autophagy triggered by CVB infection.

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Section: Introductionmentioning

confidence: 99%

Protein 2B of Coxsackievirus B3 Induces Autophagy Relying on Its Transmembrane Hydrophobic Sequences

Zhai

Chen

et al. 2016

Viruses

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“…[13][14][15] Coxsackievirus B3 (CVB3) is a small (approximately 300 Å in diameter), non-enveloped, positive-stranded RNA enterovirus associated with a number of diverse syndromes including viral myocarditis, hepatitis, pancreatitis, virus-induced heart disease and meningitis in humans. 8,[16][17][18] CVB3 related diseases are the cause of approximately 50% of the heart transplantations registered annually worldwide. The CVB3 genome is 7.4 kb long and contains untranslated regions (UTRs) at its both 5 0 and 3 0 ends (Fig.…”

Section: Introductionmentioning

confidence: 99%

Effect of T68A/N126Y mutations on the conformational and ligand binding landscape of Coxsackievirus B3 3C protease

Bhakat

2015

Mol. BioSyst.

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3C protease of Coxsackievirus B3 (CVB3) plays an essential role in the viral replication cycle, and therefore, emerged as an attractive therapeutic target for the treatment of human diseases caused by CVB3 infection. In this study, we report the first account of the molecular impact of the T68A/N126Y double mutant (Mutant(Bound)) using an integrated computational approach. Molecular dynamics simulation and post-dynamics binding free energy, principal component analysis (PCA), hydrogen bond occupancy, SASA, R(g) and RMSF confirm that T68A/N126Y instigated an increased conformational flexibility due to the loss of intra- and inter-molecular hydrogen bond interactions and other prominent binding forces, which led to a decreased protease grip on the ligand (3CPI). The double mutations triggered a distortion orientation of 3CPI in the active site and decreases the binding energy, ΔG(bind) (∼3 kcal mol(-1)), compared to the wild type (Wild(Bound)). The van der Waals and electrostatic energy contributions coming from residues 68 and 126 are lower for Mutant(Bound) when compared with Wild(Bound). In addition, variation in the overall enzyme motion as evident from the PCA, distorted hydrogen bonding network and loss of protein-ligand interactions resulted in a loss of inhibitor efficiency. The comprehensive molecular insight gained from this study should be of great importance in understanding the drug resistance against CVB3 3C protease; also, it will assist in the designing of novel Coxsackievirus B3 inhibitors with high ligand efficacy on resistant strains.

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Semaphorin7A aggravates coxsackievirusB3-induced viral myocarditis by increasing α1β1-integrin macrophages and subsequent enhanced inflammatory response

Meng

Wang

et al. 2018

Journal of Molecular and Cellular Cardiology

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RETRACTED: Antiviral and myocyte protective effects of IL-28A in coxsackievirus B3-induced myocarditis

Abstract: The antiviral and myocyte protective effects of IL-28A in CVB3-induced myocarditis are regulated by STAT1 and STAT2.

Cited by 3 publications

References 47 publications

Protein 2B of Coxsackievirus B3 Induces Autophagy Relying on Its Transmembrane Hydrophobic Sequences

Protein 2B of Coxsackievirus B3 Induces Autophagy Relying on Its Transmembrane Hydrophobic Sequences

Effect of T68A/N126Y mutations on the conformational and ligand binding landscape of Coxsackievirus B3 3C protease

Semaphorin7A aggravates coxsackievirusB3-induced viral myocarditis by increasing α1β1-integrin macrophages and subsequent enhanced inflammatory response

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