RESEARCH: EBOLA
FOLDING PROJECT #16460 PROFILE

This project looks at a mutated part of the Ebola virus protein that stops it from working properly. The mutation prevents the virus from interacting with its own RNA, making it less dangerous. Scientists hope to use this information to design drugs that block the virus's activity in a similar way.

This project simulates the F239A mutant of the immune inhibitory domain from the Ebola virus viral protein 35 (VP35), which is critical for viral infection.

This protein helps the virus escape detection inside human cells.

The F239A mutant being simulated here is unable to interact with other viral components such as RNA.

This makes its dynamics of particular interest such that if we can design a drug to affect protein function similarly to this mutation, we may be able to counteract the virus's effect.

Ebola virus

A hemorrhagic fever caused by the Ebola virus.

Ebola virus is a highly contagious and deadly virus that causes severe hemorrhagic fever. Symptoms include fever, muscle pain, vomiting, diarrhea, and internal bleeding. There is no cure for Ebola, but supportive care can improve survival rates.

Protein

Large biomolecules essential for all biological processes.

Proteins are the workhorses of cells, carrying out a wide range of functions. They are made up of chains of amino acids and play vital roles in everything from digestion to immune response.

Viral protein 35 (VP35)

A viral protein involved in immune evasion.

VP35 is a protein found in the Ebola virus. It plays a crucial role in helping the virus evade the host's immune system by interfering with signaling pathways that would otherwise trigger an antiviral response.

Mutation

A permanent change in the DNA sequence.

Mutations are alterations in the genetic code that can lead to changes in protein structure and function. Some mutations are harmful, while others can be beneficial or have no effect.

F239A mutant

A specific mutation in the Ebola virus VP35 protein.

The F239A mutant is a specific alteration in the amino acid sequence of the VP35 protein. This change affects the protein's ability to interact with other viral components and potentially weakens the virus's ability to infect cells.