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M Protein from Dengue virus oligomerizes to pentameric channel protein: in silico analysis study

Zeba, A and Sekar, K and Ganjiwale, A (2023) M Protein from Dengue virus oligomerizes to pentameric channel protein: in silico analysis study. In: Genomics and Informatics, 21 (3).

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Official URL: https://doi.org/10.5808/gi.23035


The Dengue virus M protein is a 75 amino acid polypeptide with two helical transmem-branes (TM). The TM domain oligomerizes to form an ion channel, facilitating viral release from the host cells. The M protein has a critical role in the virus entry and life cycle, making it a potent drug target. The oligomerization of the monomeric protein was studied using ab initio modeling and molecular dynamics simulation in an implicit membrane environment. The representative structures obtained showed pentamer as the most stable oligomeric state, resembling an ion channel. Glutamic acid, threonine, serine, tryptophan, alanine, iso-leucine form the pore-lining residues of the pentameric channel, conferring an overall negative charge to the channel with approximate length of 51.9 à . Residue interaction analysis for M protein shows that Ala94, Leu95, Ser112, Glu124, and Phe155 are the central hub residues representing the physicochemical interactions between domains. The virtual screening with 165 different ion channel inhibitors from the ion channel library shows monovalent ion channel blockers, namely lumacaftor, glipizide, gliquidone, glisoxepide, and azelnidipine to be the inhibitors with high docking scores. Understanding the three-dimen-sional structure of M protein will help design therapeutics and vaccines for Dengue infection. © 2023 Korea Genome Organization.

Item Type: Journal Article
Publication: Genomics and Informatics
Publisher: Korea Genome Organization
Additional Information: The copyright for this article belongs to the Authors.
Department/Centre: Division of Interdisciplinary Sciences > Computational and Data Sciences
Date Deposited: 17 Dec 2023 07:03
Last Modified: 17 Dec 2023 07:03
URI: https://eprints.iisc.ac.in/id/eprint/83428

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