NEW YORK (Reuters Health) - The HIV myristoylated matrix protein (myr-MA) is a molecular switch that plays an important role in the intracellular localization of the virus. Now new research suggests that this switch works quite differently from other myristyl switches that are regulated by mechanically induced conformational changes.
HIV myr-MA either directs the Gag polyprotein to the plasma membrane during viral assembly or promotes its release from the membrane to facilitate nuclear targeting. However, it was unclear exactly how these functions were regulated.
Dr. Michael F. Summers, from the University of Maryland in Baltimore, and colleagues found that in contrast to other myristyl switches, HIV myr-MA is not regulated by mechanically induced conformational changes. Instead, the association of other Gag subdomains seems to determine the functional state of the switch.
The new findings are based on a study reported in the December 26th issue of the Proceedings of the National Academy of Sciences.
“The structural information should facilitate efforts to develop therapeutic strategies that target the HIV-1 myristyl signal,” the investigators conclude.
Proc Natl Acad Sci USA 2003;December 26th online issue.
MeSH Headings:Myristates: Myristic Acids: Retroviridae Proteins: Viral Core Proteins: Viral Proteins: Viral Structural Proteins: Gene Products, gag: Nucleocapsid Proteins: PolyproteinsCopyright © 2002 Reuters Limited. All rights reserved. Republication or redistribution of Reuters content, including by framing or similar means, is expressly prohibited without the prior written consent of Reuters. Reuters shall not be liable for any errors or delays in the content, or for any actions taken in reliance thereon. Reuters and the Reuters sphere logo are registered trademarks and trademarks of the Reuters group of companies around the world.
