In silico comparative structural and compositional analysis of glycoproteins of RSV to study the nature of stability and transmissibility of RSV A  

作　　者：Debanjan Mitra Pradeep K.Das Mohapatra 

机构地区：[1]Department of Microbiology,Raiganj University,Raiganj,WB,India

出　　处：《Systems Microbiology and Biomanufacturing》2023年第2期312-327,共16页系统微生物学与生物制造（英文）

摘　　要：The current scenario of COVID-19 makes us to think about the devastating diseases that kill so many people every year.Analysis of viral proteins contributes many things that are utterly useful in the evolution of therapeutic drugs and vaccines.In this study,sequence and structure of fusion glycoproteins and major surface glycoproteins of respiratory syncytial virus(RSV)were analysed to reveal the stability and transmission rate.RSV A has the highest abundance of aromatic residues.The Kyte–Doolittle scale indicates the hydrophilic nature of RSV A protein which leads to the higher transmission rate of this virus.Intra-protein interactions such as carbonyl interactions,cation-pi,and salt bridges were shown to be greater in RSV A compared to RSV B,which might lead to improved stability.This study discovered the presence of a network aromatic–sulphur interaction in viral proteins.Analysis of ligand binding pocket of RSV proteins indicated that drugs are performing better on RSV B than RSV A.It was also shown that increasing the number of tunnels in RSV A proteins boosts catalytic activity.This study will be helpful in drug discovery and vaccine development.

关 键 词：Respiratory syncytial virus Stability Intra-protein interactions TUNNELS Drug discovery 

分 类 号：Q816[生物学—生物工程]