Article

Mutation of Ebola Virus Matrix Protein Cysteine Residues Increases Binding to Phosphatidylserine through Increased Flexibility of a Lipid Binding Loop

2018-03-21

Abstract excerpt

The Ebola virus (EBOV) is a genetically simple negative sense RNA virus with only 7 genes yet it causes severe hemorrhagic fever in humans. The matrix protein VP40 of EBOV is the main driver of viral budding through binding to host plasma membrane lipids and formation of the filamentous, pleomorphic virus particles. To better understand this dynamic and complex process we have asked what the role of two highly con...

Topics

Open a Topic to create a Post that cites this publication.

Identifiers and source

Literature Corpus work: 7b8d88f7-becf-5282-88fc-faaa4a5be0b8
DOI: 10.1101/286120

Open publication

Related research

Semantic proximity does not establish scientific evidence.

Click a neighbor to travelStep 1 · 12 closest

Mutation of Ebola Virus Matrix Protein Cysteine Residues Increases Binding to Phosphatidylserine through Increased Flexibility of a Lipid Binding LoopDOI 10.1101/286120Read

Cysteine Mutations in the Ebolavirus Matrix Protein VP40 Promote Phosphatidylserine Binding by Increasing the Flexibility of a Lipid-Binding Loop.Semantic proximity Read

Minor electrostatic changes robustly increase VP40 membrane binding, assembly, and budding of Ebola virus matrix protein derived virus-like particles.Semantic proximity Read

Variants of the Ebola virus matrix protein VP40 have differential effects on oligomerization and plasma membrane interactions.Semantic proximity Read

Ebola Virus Matrix Protein VP40 Single Mutations G198R and G201R Significantly Enhance Plasma Membrane Localization.Semantic proximity Read

A cationic, C-terminal patch and structural rearrangements in Ebola virus matrix VP40 protein control its interactions with phosphatidylserine.Semantic proximity Read

Mutation of Hydrophobic Residues in the C-Terminal Domain of the Marburg Virus Matrix Protein VP40 Disrupts Trafficking to the Plasma Membrane.Semantic proximity Read

A loop region in the N-terminal domain of Ebola virus VP40 is important in viral assembly, budding, and egress.Semantic proximity Read

Interaction of monomeric Ebola VP40 protein with a plasma membrane: A coarse-grained molecular dynamics (CGMD) simulation study.Semantic proximity Read

Did a Single Amino Acid Change Make Ebola Virus More Virulent?Semantic proximity Read

Non-active site mutations disturb the loop dynamics, dimerization, viral budding and egress of VP40 of the Ebola virus.Semantic proximity Read

Cryo-EM structure of Sudan ebolavirus glycoprotein complexed with its human endosomal receptor NPC1Semantic proximity Read

Mechanisms of phosphatidylserine influence on viral production: a computational model of Ebola virus matrix protein assemblySemantic proximity Read