Authors:

Manuel Torres Narvaez

Date Created:

Not specified

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About Paper:

In 1976 a new virus was discovered, the Ebola Virus (EBOV). This microorganism is part of the Filoviridae family, a filamentous virus with a lipid-envelope, which is extracted from the plasma membrane of the host cell during infection. The EBOV genome is a negative sense RNA, which means the EBOV can replicate more easily in the cytoplasm of the infected cell. EBOV can cause a hemorrhagic fever with a high fatality rate and is classified as a category A pathogen by the National Institutes of Health. It is important to know how the EBOV proteins work, so a therapeutic target can be developed. This paper will be focused on the function of the matrix protein of EBOV known as viral protein 40kDa (eVP40). eVP40 can influence the regulation of gene expression, the formation of virus assembly and budding from the host cell. Additionally, it has been seen that eVP40 is sufficient to form virus-like particles in the absence of other EBOV proteins. The way of investigating eVP40 interactions will be by inducing amino acid mutations in key regions of the protein to determine the presence of different eVP40 conformations, monomer, dimer, or octamer. These different conformations have been linked to different steps of the virus life cycle. Is expected that if the mutations work the presence and amount of these conformations in the host cells will change. This work could help to develop small molecules or antibodies that alter the VP40 conformations as a way to provide a potential treatment.

Source:

Purdue University / 2023

Topics:

No topics listed

Co-authors:

Manuel Torres Narvaez