The Effects of SARS CoV-2 nsp13 Mutations on the Structure and Stability of Helicase in Chinese Isolates

Basit Öğe Kaydı
dc.authorid0000-0002-7526-9835en_US
dc.contributor.authorAkbulut, Ekrem
dc.date.accessioned2022-07-25T05:51:48Z
dc.date.available2022-07-25T05:51:48Z
dc.date.issued2022en_US
dc.departmentMTÖ Üniversitesi, Mühendislik ve Doğa Bilimleri Fakültesi, Biyomühendislik Bölümüen_US
dc.descriptionSubmitted: 23.01.2022, Revision Requested: 17.02.2022, Last Revision Received: 19.02.2022, Accepted: 21.03.2022, Published Online: 13.04.2022.en_US
dc.descriptionContent of this journal is licensed under a Creative Commons Attribution-NonCommercial 4.0 International License.en_US
dc.description.abstractObjective: Coronavirus Disease 2019 (COVID19) is a viral disease caused by Severe Acute Respiratory Syndrome Coronavirus-2 (SARS CoV-2). The high mutation propensity of the SARS CoV-2 genome is one of the biggest threats to the long-term validity of treatment options. Helicases are anti-viral targets because of the vital role they play in the viral life cycle. In this study, changes in the protein structure caused by SARS CoV-2 nsp13 mutations were investigated to contribute to the development of effective antiviral drugs. Materials and Methods: Genome data of 298 individuals located in the China location were examined. The mutant model was built using deep learning algorithms. Model quality assessment was done with QMEAN. Protein stability analyses were performed with DynaMut2 and Cutoff Scanning Matrix stability. Changes in substrate affinity were performed with Haddock v2.4. Results: In this study, twenty-eight mutations in nsp13 were identified (23 sense, 5 missense). The changes in protein structure caused by the five missense mutations (Leu14Phe, Arg15Ser, Arg21Ser, Leu235Phe, Ala454Thr) were modeled. The mutations caused a decrease in the stability of SARS CoV-2 helicase (-0.99, -1.66, -1.15, -0.54, and -0.73 for Leu14Phe, Arg15Ser, Arg21Ser, Leu235Phe, Ala454Thr, respectively). The mutations reduced the helicase's affinity to the substrate. The docking scores for wild-type and mutant helicase were -84.4±1.4 kcal.mol-1 and -71.1±6.7 kcal.mol-1, respectively. Conclusion: Helicase mutations caused a decrease in the protein stability and nucleic acid affinity of the SARS CoV-2 helicase. The results provide important data on the development of potential antivirals and the effect of mutation on the functions of viral proteins.en_US
dc.identifier.citationAkbulut, E. (2019). The Effects of SARS CoV-2 nsp13 Mutations on the Structure and Stability of Helicase in Chinese Isolates. European Journal of Biology.en_US
dc.identifier.doi10.26650/EurJBiol.2022.1061858
dc.identifier.endpage17en_US
dc.identifier.issn2602-2575en_US
dc.identifier.issn2618-6144en_US
dc.identifier.issue1en_US
dc.identifier.scopus2-s2.0-85133881301en_US
dc.identifier.scopusqualityQ4en_US
dc.identifier.startpage11en_US
dc.identifier.urihttps://doi.org/10.26650/EurJBiol.2022.1061858
dc.identifier.urihttps://hdl.handle.net/20.500.12899/1174
dc.identifier.volume81en_US
dc.indekslendigikaynakScopusen_US
dc.institutionauthorAkbulut, Ekrem
dc.language.isoenen_US
dc.publisherİstanbul Üniversitesi / İstanbul Universityen_US
dc.relation.ispartofEuropean Journal of Biologyen_US
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.rightsinfo:eu-repo/semantics/openAccessen_US
dc.subjectCOVID19en_US
dc.subjectHelicaseen_US
dc.subjectMutationen_US
dc.subjectProtein stabilityen_US
dc.subjectSARS CoV-2 genomeen_US
dc.subjectSubstrate affinityen_US
dc.subject.otherCOVID-19en_US
dc.titleThe Effects of SARS CoV-2 nsp13 Mutations on the Structure and Stability of Helicase in Chinese Isolatesen_US
dc.typeArticleen_US

Dosyalar

Orijinal paket
Listeleniyor 1 - 1 / 1
Küçük Resim
İsim:
Ekrem Akbulut - Makale Dosyası.pdf
Boyut:
2.01 MB
Biçim:
Adobe Portable Document Format
Açıklama:
Full Text / Tam Metin
İndir
Lisans paketi
Listeleniyor 1 - 1 / 1
Küçük Resim Yok
İsim:
license.txt
Boyut:
1.44 KB
Biçim:
Item-specific license agreed upon to submission
Açıklama:
İndir

Koleksiyon

Biyomühendislik Bölümü Koleksiyonu
Scopus İndeksli Yayınlar Koleksiyonu