biostudies-literatureHamza ACouncil of Scientific and Industrial ResearchCentral Council for Research in Unani Medicine1950https://www.ebi.ac.uk/biostudies/studies/S-EPMC8880246biostudies-literatureUnknown23(4)Respiratory syncytial virus (RSV) is the leading cause of lower respiratory tract infection in children and infants. To date, there is no effective vaccine available against RSV. Heparan sulfate is a type of glycosaminoglycan that aids in the attachment of the RSV to the host cell membrane via the G protein. In the present study, the effect of amino acid substitution on the structure and stability of the ectodomain G protein was studied. Further, it was investigated whether mutation (K117A) in the CX3C motif of G protein alters the binding with heparan sulfate. The point mutation significantly affects the conformational stability of the G protein. The mutant protein showed a low binding affinity with heparan sulfate as compared to the wild-type G protein, as determined by fluorescence quenInternational journal of molecular sciencesMutation in the CX3C Motif of G Protein Disrupts Its Interaction with Heparan Sulfate: A Calorimetric, Spectroscopic, and Molecular Docking Study.PMC8880246RG-1439-7437(1697)17/EMR-IIF.No.3-63/2019-CCRUM/TechHamza AAlmajhdi FNHussain TParveen SAra SAhmed ASamad AIslam AParray ZAfalseMutation in the CX3C Motif of G Protein Disrupts Its Interaction with Heparan Sulfate: A Calorimetric, Spectroscopic, and Molecular Docking Study.Respiratory syncytial virus (RSV) is the leading cause of lower respiratory tract infection in children and infants. To date, there is no effective vaccine available against RSV. Heparan sulfate is a type of glycosaminoglycan that aids in the attachment of the RSV to the host cell membrane via the G protein. In the present study, the effect of amino acid substitution on the structure and stability of the ectodomain G protein was studied. Further, it was investigated whether mutation (K117A) in the CX3C motif of G protein alters the binding with heparan sulfate. The point mutation significantly affects the conformational stability of the G protein. The mutant protein showed a low binding affinity with heparan sulfate as compared to the wild-type G protein, as determined by fluorescence quen2022-01-01T00:00:00Z2022 Feb2025-04-19T10:50:55.362Z2024-11-15T00:29:13.257ZS-EPMC88802463521606610.3390/ijms23041950