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Structural exploration of Y-domain reveals its essentiality in HEV pathogenesis.
Shafat, Zoya; Hamza, Abu; Islam, Asimul; Al-Dosari, Mohammed S; Parvez, Mohammad K; Parveen, Shama.
Afiliación
  • Shafat Z; Centre for Interdisciplinary Research in Basic Sciences, Jamia Millia Islamia, New Delhi, India.
  • Hamza A; Centre for Interdisciplinary Research in Basic Sciences, Jamia Millia Islamia, New Delhi, India.
  • Islam A; Centre for Interdisciplinary Research in Basic Sciences, Jamia Millia Islamia, New Delhi, India.
  • Al-Dosari MS; Department of Pharmacognosy, College of Pharmacy, King Saud University, Riyadh, Saudi Arabia.
  • Parvez MK; Department of Pharmacognosy, College of Pharmacy, King Saud University, Riyadh, Saudi Arabia. Electronic address: mohkhalid@ksu.edu.sa.
  • Parveen S; Centre for Interdisciplinary Research in Basic Sciences, Jamia Millia Islamia, New Delhi, India. Electronic address: sparveen2@jmi.ac.in.
Protein Expr Purif ; 187: 105947, 2021 11.
Article en En | MEDLINE | ID: mdl-34314826
Hepatitis E virus (HEV) is a major causative agent of hepatitis E infections across the globe. Although the essentiality of HEV nonstructural polyprotein (pORF1) putative Y-domain (Yd) has been established in viral pathogenesis, its structural-functional role remains elusive. The current research discusses the novel exploration on Yd protein expression, purification, biophysical characterization and structure-based docking analysis. The codon optimized synthetic gene and optimized expression parameters i.e., 5 h induction with 0.25 mM IPTG at 37 °C, resulted in efficient production of Yd protein (~40 kDa) in E. coli BL21(DE3) cells. Majority of the recombinant Yd (rYd) protein expressed as inclusion bodies was solubilized in 0.5% N-lauroylsarcosine and purified using Ni-NTA chromatography. Circular dichroism (CD) and UV visible absorption spectroscopic studies on Yd revealed both secondary and tertiary structure stability in alkaline range (pH 8.0-10.0), suggesting correlation with its physiological activity. Thus, loss in structure at low pH perhaps play crucial role in cytoplasmic-membrane interaction. The biophysical data were in good agreement with insilico structural analyses, which suggested mixed α/ß fold, non-random and basic nature of Yd protein. Furthermore, due to Yd protein essentiality in HEV replication and pathogenesis, it was considered as a template for docking and drug-likeness analyses. The 3D modeling of Yd protein and structure-based screening and drug-likeness of inhibitory compounds, including established antiviral drugs led to the identification of top nine promising candidates. Nonetheless, in vitro studies on the predicted interaction of Yd with intracellular-membrane towards establishing replication-complexes as well as validations of the proposed therapeutic agents are warranted.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Proteínas Virales / Proteínas Recombinantes / Virus de la Hepatitis E Tipo de estudio: Etiology_studies / Prognostic_studies Límite: Humans Idioma: En Revista: Protein Expr Purif Asunto de la revista: BIOLOGIA MOLECULAR Año: 2021 Tipo del documento: Article País de afiliación: India Pais de publicación: Estados Unidos

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Proteínas Virales / Proteínas Recombinantes / Virus de la Hepatitis E Tipo de estudio: Etiology_studies / Prognostic_studies Límite: Humans Idioma: En Revista: Protein Expr Purif Asunto de la revista: BIOLOGIA MOLECULAR Año: 2021 Tipo del documento: Article País de afiliación: India Pais de publicación: Estados Unidos