Depicting Molecular
Interactions of Luteolin with Human Cytomegalovirus Envelope Glycoprotein N and
Glycoprotein H: An In Silico Approach
Nayak Subham Ravi, Tripathy Chandra Sekhar, Parida Sagarika, Pattnaik Dipti and
Patro A. Raj Kumar
Res. J. Biotech.; Vol. 21(2); 33-40;
doi: https://doi.org/10.25303/212rjbt033040; (2026)
Abstract
Human cytomegalovirus (HCMV) poses a significant threat causing congenital viral
infection in new-borns and in individuals with weakened immune system. The rise
of drug resistance in one or more approved antiviral medications, has created an
urgent need for the development of the new antiviral medications. This study explored
the role of a plant-derived flavonoid luteolin, as a potential antiviral agent targeting
human cytomegalovirus glycoproteins N and H by molecular docking. Using computational
methods, we investigated luteolin's interaction with two key HCMV envelope glycoprotein
N (UniProt ID:F5HHQ0) and envelope glycoprotein H (UniProt ID:Q6SW67). Molecular
docking performed with AutoDock Vina 4.2 predicted binding affinities and assessed
luteolin's drug-likeness using Lipinski's Rule of Five via SwissADME. Luteolin demonstrated
higher binding affinities of -6.4 kcal/mol binding energy with Envelope glycoprotein
N, forming hydrogen bonds with Thr52(A), Thr135(A) and Cys116(A)
Against Envelope glycoprotein H, luteolin has a stronger binding affinity of -7.1
kcal/mol, interacting with Ser577(A) (two bonds) and Ile666(A). Notably, luteolin
met Lipinski's criteria for drug-likeness. This study highlights luteolin as a promising
novel antiviral against human cytomegalovirus, exhibiting higher binding affinities
to envelope glycoproteins. This warrants further experimental investigation to investigate
the efficacy of luteolin as a potential antiviral agent against HCMV.
