Researcher:
Vatansever, Sezen

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PhD Student

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Sezen

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Vatansever

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Vatansever, Sezen

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2015 - 20184

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    The interplay between viperin antiviral activity, lipid droplets and junin mammarenavirus multiplication
    (Elsevier, 2018) Pena Carcamo, Jose R.; Morell, Maria L.; Vazquez, Cecilia A.; Upadhyay, Arunkumar S.; Overby, Anna K.; Cordo, Sandra M.; Garcia, Cybele C.; Vatansever, Sezen; PhD Student; Graduate School of Sciences and Engineering; N/A
    Junin arenavirus infections are associated with high levels of interferons in both severe and fatal cases. Upon Junin virus (JUNV) infection a cell signaling cascade initiates, that ultimately attempts to limit viral replication and prevent infection progression through the expression of host antiviral proteins. The interferon stimulated gene (ISG) viperin has drawn our attention as it has been highlighted as an important antiviral protein against several viral infections. The studies of the mechanistic actions of viperin have described important functional domains relating its antiviral and immune-modulating actions through cellular lipid structures. In line with this, through silencing and overexpression approaches, we have identified viperin as an antiviral ISG against JUNV. In addition, we found that lipid droplet structures are modulated during JUNV infection, suggesting its relevance for proper virus multiplication. Furthermore, our confocal microscopy images, bioinformatics and functional results also revealed viperin-JUNV protein interactions that might be participating in this antiviral pathway at lipid droplet level. Altogether, these results will help to better understand the factors mediating innate immunity in arenavirus infection and may lead to the development of pharmacological agents that can boost their effectiveness thereby leading to new treatments for this viral disease.
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    Viperin exerts antiviral function against junin mammarenavirus at different subcellular localizations.
    (Amer Soc Cell Biology, 2017) Morell, M. L.; Pena Carcamo, J. R.; Vazquez, C. A.; Upadhyay, A. S.; Overby, A. K.; Cordo, S. M.; Garcia, C. C.; Vatansever, Sezen; PhD Student; Graduate School of Sciences and Engineering; N/A
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    PublicationOpen Access
    Antiviral activity of an N-allyl acridone against dengue virus
    (BioMed Central, 2015) Mazzucco, Maria B.; Talarico, Laura B.; Carro, Ana C.; Fascio, Mirta L.; D'Accorso, Norma B.; Garcia, Cybele C.; Damonte, Elsa B.; N/A; Vatansever, Sezen; PhD Student; Graduate School of Sciences and Engineering
    Background: Dengue virus (DENV), a member of the family Flaviviridae, is at present the most widespread causative agent of a human viral disease transmitted by mosquitoes. Despite the increasing incidence of this pathogen, there are no antiviral drugs or vaccines currently available for treatment or prevention. In a previous screening assay, we identified a group of N-allyl acridones as effective virus inhibitors. Here, the antiviral activity and mode of action targeted to viral RNA replication of one of the most active DENV-2 inhibitors was further characterized. Results: The compound 10-allyl-7-chloro-9(10H)-acridone, designated 3b, was active to inhibit the in vitro infection of Vero cells with the four DENV serotypes, with effective concentration 50% (EC50) values in the range 12.5-27.1 mu M, as determined by virus yield inhibition assays. The compound was also effective in human HeLa cells. No cytotoxicity was detected at 3b concentrations up to 1000 mu M. Mechanistic studies demonstrated that virus entry into the host cell was not affected, whereas viral RNA synthesis was strongly inhibited, as quantified by real time RT-PCR. The addition of exogenous guanosine together with 3b rescued only partially the infectivity of DENV-2. Conclusions: The acridone derivative 3b selectively inhibits the infection of Vero cells with the four DENV serotypes without a direct interaction with the host cell or the virion but interfering specifically with the intracellular virus multiplication. The mode of antiviral action for this acridone apparently involves the cellular enzyme inosine-monophospahe dehydrogenase together with another still unidentified target related to DENV RNA synthesis.
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    PublicationOpen Access
    Intrinsic K-Ras dynamics: a novel molecular dynamics data analysis method shows causality between residue pair motions
    (Nature Publishing Group (NPG), 2016) Gumus, Zeynep H.; Department of Chemical and Biological Engineering; Vatansever, Sezen; Erman, Burak; PhD Student; Faculty Member; Department of Chemical and Biological Engineering; College of Engineering; N/A; 179997
    K-Ras is the most frequently mutated oncogene in human cancers, but there are still no drugs that directly target it in the clinic. Recent studies utilizing dynamics information show promising results for selectively targeting mutant K-Ras. However, despite extensive characterization, the mechanisms by which K-Ras residue fluctuations transfer allosteric regulatory information remain unknown. Understanding the direction of information flow can provide new mechanistic insights for K-Ras targeting. Here, we present a novel approach - conditional time-delayed correlations (CTC) - using the motions of all residue pairs of a protein to predict directionality in the allosteric regulation of the protein fluctuations. Analyzing nucleotide-dependent intrinsic K-Ras motions with the new approach yields predictions that agree with the literature, showing that GTP-binding stabilizes K-Ras motions and leads to residue correlations with relatively long characteristic decay times. Furthermore, our study is the first to identify driver-follower relationships in correlated motions of K-Ras residue pairs, revealing the direction of information flow during allosteric modulation of its nucleotide-dependent intrinsic activity: active K-Ras Switch-II region motions drive Switch-I region motions, while alpha-helix-3L7 motions control both. Our results provide novel insights for strategies that directly target mutant K-Ras.