The crux and crust of ebolavirus: Analysis of genome sequences and glycoprotein gene

Mahale, Kiran N.; Patole, Milind S.

doi:10.1016/j.bbrc.2015.06.008

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Differences That May Contribute To Pathogenicity1

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Cited by 3 publications

(1 citation statement)

References 26 publications

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“…At 37 kDa, RESTV ssGP is significantly larger than that of the other Ebolaviruses (33 kDa). However, the potential involvement of ssGP in pathogenicity remains unclear and thus the effect of the RESTV ssGP extension is unknown (60). …”

Section: Differences That May Contribute To Pathogenicitymentioning

confidence: 99%

Risks Posed by Reston, the Forgotten Ebolavirus

Cantoni

Hamlet

Michaelis

et al. 2016

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Section: Differences That May Contribute To Pathogenicitymentioning

confidence: 99%

Risks Posed by Reston, the Forgotten Ebolavirus

Cantoni

Hamlet

Michaelis

et al. 2016

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Human transmission of Ebola virus

Lawrence

Danet

Reynard

et al. 2017

Current Opinion in Virology

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Ebolavirus interferon antagonists—protein interaction perspectives to combat pathogenesis

Banerjee

Pal

et al. 2017

Briefings in Functional Genomics

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Zaire ebolavirus, one of the most pathogenic species of Ebolavirus, is a significant threat to the human community being both highly infectious and lethal. The viral proteins (VPs), specifically VP24 and VP35, antagonize the interferon (IFN) proteins accountable for human immune response. Several efforts have been made to design vaccines and therapeutics drugs. However, the success is not encouraging because of limited knowledge about the binding site information of the VPs. Such limitations stem largely from the highly infectious nature of the virus that requires specialized personnel and biosafety laboratories. As an alternative, computational techniques have also been adopted to improve the success rate of drug discovery. This article elaborates on the interactions between viral and human IFN proteins that lead to IFN antagonism. A computational framework is proposed after evaluating existing computational studies. This protein interaction and protein design-based computational framework identified critical interacting residues of the VP (VP24) responsible for the formation of a stable complex with the human KPNA5 (karyopherin alpha proteins 5). The mutations of those critical residues, as demonstrated in this article, affected the overall stability of the complex because of a sharp decrease in both the number of hydrogen bonds and possible charge-charge interactions. Therefore, we proposed that the framework could be an effective alternative to experimental work for destabilizing interactions between the VPs and human proteins responsible for IFN induction and response.

show abstract

The crux and crust of ebolavirus: Analysis of genome sequences and glycoprotein gene

Cited by 3 publications

References 26 publications

Risks Posed by Reston, the Forgotten Ebolavirus

Risks Posed by Reston, the Forgotten Ebolavirus

Human transmission of Ebola virus

Ebolavirus interferon antagonists—protein interaction perspectives to combat pathogenesis

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