Your browser doesn't support javascript.
D155Y substitution of SARS-CoV-2 ORF3a weakens binding with Caveolin-1.
Gupta, Suchetana; Mallick, Ditipriya; Banerjee, Kumarjeet; Mukherjee, Shrimon; Sarkar, Soumyadev; Lee, Sonny Tm; Basuchowdhuri, Partha; Jana, Siddhartha S.
  • Gupta S; School of Mathematical and Computational Sciences, Indian Association for the Cultivation of Science, India.
  • Mallick D; School of Biological Sciences, Indian Association for the Cultivation of Science, India.
  • Banerjee K; School of Biological Sciences, Indian Association for the Cultivation of Science, India.
  • Mukherjee S; School of Mathematical and Computational Sciences, Indian Association for the Cultivation of Science, India.
  • Sarkar S; Division of Biology, Kansas State University, USA.
  • Lee ST; Division of Biology, Kansas State University, USA.
  • Basuchowdhuri P; School of Mathematical and Computational Sciences, Indian Association for the Cultivation of Science, India.
  • Jana SS; School of Biological Sciences, Indian Association for the Cultivation of Science, India.
Comput Struct Biotechnol J ; 20: 766-778, 2022.
Article in English | MEDLINE | ID: covidwho-2261663
ABSTRACT
The clinical manifestation of the recent pandemic COVID-19, caused by the novel SARS-CoV-2 virus, varies from mild to severe respiratory illness. Although environmental, demographic and co-morbidity factors have an impact on the severity of the disease, contribution of the mutations in each of the viral genes towards the degree of severity needs a deeper understanding for designing a better therapeutic approach against COVID-19. Open Reading Frame-3a (ORF3a) protein has been found to be mutated at several positions. In this work, we have studied the effect of one of the most frequently occurring mutants, D155Y of ORF3a protein, found in Indian COVID-19 patients. Using computational simulations we demonstrated that the substitution at 155th changed the amino acids involved in salt bridge formation, hydrogen-bond occupancy, interactome clusters, and the stability of the protein compared with the other substitutions found in Indian patients. Protein-protein docking using HADDOCK analysis revealed that substitution D155Y weakened the binding affinity of ORF3a with caveolin-1 compared with the other substitutions, suggesting its importance in the overall stability of ORF3a-caveolin-1 complex, which may modulate the virulence property of SARS-CoV-2.
Keywords

Full text: Available Collection: International databases Database: MEDLINE Type of study: Prognostic study Language: English Journal: Comput Struct Biotechnol J Year: 2022 Document Type: Article Affiliation country: J.csbj.2022.01.017

Similar

MEDLINE

...
LILACS

LIS


Full text: Available Collection: International databases Database: MEDLINE Type of study: Prognostic study Language: English Journal: Comput Struct Biotechnol J Year: 2022 Document Type: Article Affiliation country: J.csbj.2022.01.017