Publication Highlight
Getting a clearer view of RSV
Disclaimer: This publication highlight is part of the SBGrid/Meharry Medical College Communities Project, focused on science education and demonstrating how structural biology and preclinical science connect to medicine.
Respiratory syncytial virus (RSV) can cause serious illness to young children and elderly populations. For this reason, it is highly recommended that all people coming in contact with at-risk populations receive a vaccination against this prolific virus; especially for those who are caring for or engaging with newborn babies. RSV is in the order of Mononegavirales viruses that all tend to have high infection rates and poor clinical outcomes, like ebola, measles, and rabies. This family of viruses share similar structures and key participating proteins. Understanding how these viruses form and the machinery they use to carry out infection is of great importance to virologists and epidemiologists alike.
In a recent paper in Nature Communications, SBGrid member Dr. Elizabeth Wright, gains atomic level observations on the structure of RSV. Using a powerful microscopic technique called cryogenic electron tomography (Cryo-ET), Dr. Wright is able to look at the building blocks that hold RSV together. She finds that the internal envelope of RSV is composed of tightly packed helices of a matrix protein. This structure is reminiscent of the outer layer of the cotton string that is wrapped around a baseball before the final outer layer of leather is added. Dr. Wright and her collaborators also found that the fusion protein that is presented on the outside of the virus and is the target of most vaccines is commonly found in dimer-of-trimer configurations. These discoveries could help with the creation of new vaccines for RSV and provide better understanding of the structure of Mononegavirales viruses.
Read more in Nature Communications
By Vida Robertson, Fisk University
Vida Storm Robertson is a Masters Student in Chemistry at Fisk University working in both solid-state and solution based structural determination techniques. He began his PhD in Biochemistry and Molecular Biophysics at Caltech this summer.
