Abstract：
:Dengue virus (DENV) is an emerging health threat and its envelope glycoprotein E, is involved in the anchoring and fusion mechanisms. Anchoring followed by conformational changes of E-protein are responsible for the fusion and entry of DENV into host. The variation in the conformation of the E-protein due to mutations, results in its altered binding with antibodies (Abs) and also its receptors. This leads to failure of neutralization of DENV and enhance the infection. In our earlier studies we have identified T219A mutation in the E-protein of DENV and the present study is focused on the impact of this mutation on the conformation of E-protein and also its binding variation with Abs and Fc-γ receptor. A comparative molecular modelling studies of wild type and T219A mutant E-proteins revealed that, the mutation induced several conformational variations in the E-protein and resulted in the variable binding orientation with altered affinities. Further, the mutation was also observed to enhance the fusion mechanism by Fc-γ receptors that mediate the efficient entry of DENV into host cell through altered membrane fusion mechanism. Such conformational variations of E-protein could be the responsible factors for enhanced virulence of DENV infections.
journal_name
Comput Methods Programs Biomedjournal_title
Computer methods and programs in biomedicineauthors
Kumar YN,Jeyakodi G,Kumar NP,Gunasekaran K,Jambulingam Pdoi
10.1016/j.cmpb.2020.105481subject
Has Abstractpub_date
2020-10-01 00:00:00pages
105481eissn
0169-2607issn
1872-7565pii
S0169-2607(20)30232-7journal_volume
195pub_type
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