13 April 2016

Learning how protective shells form around retroviruses

Two-dimensional solid state NMR carbon/nitrogen correlation spectrum peak assignments leading to successful determination of the RSV capsid structure. Two-dimensional solid state NMR carbon/nitrogen correlation spectrum peak assignments leading to successful determination of the RSV capsid structure.

Scientists gain new insights into how protective shells form around retrovirus genomes, advancing the search for drugs that will combat them.

First, some background

The Rous Sarcoma virus (RSV) is the archetype of the retrovirus family that includes HIV. Its genome is protected by a shell, called a capsid, formed by about 1,500 copies of a single protein. All capsid proteins share a common structure but assemble into distinct shapes when they form into shells.

What is the finding?

Using special nuclear magnetic resonance (NMR) techniques and instruments, scientists gained new insights into how these capsid proteins arrange themselves into shells.

THE TOOLS THEY USED

This research was conducted in the MagLab 800 MHz solid state NMR system, including low-E probe at the MagLab's NMR Facility.

Why is this important?

This knowledge advances our understanding of how retrovirus capsids assemble into distinct shapes, which will help in the design of antiviral drugs to disrupt them.

Who did the research?

Jaekyun Jeon1, Xin Qiao1, Ivan Hung2, Peter L. Gor'kov2, Zhehong Gan2 and Bo Chen1

1University of Central Florida; 2National High Magnetic Field Laboratory, Florida State University

Why did this research need the MagLab?

The high fields of the lab's NMR magnets, combined with specialized low-electric-field probes used to place and manipulate the specimens in that magnetic field, are critical for acquiring the resolution and sensitivity needed to target particular sites on these proteins and to learn how molecules bind together.

Details for scientists

Funding

This research was funded by the following grant: G.S. Boebinger (NSF DMR-1157490); Bo Chen (AFOSR FA9550-13-1-0150)


For more information, contact Zhehong Gan.

Details

  • Research Area: Biochemistry, Biology, Chemistry
  • Research Initiatives: Life
  • Facility / Program: NMR/MRI
  • Year: 2016
Last modified on 14 April 2016