Advertisement

If you have an ACS member number, please enter it here so we can link this account to your membership. (optional)

ACS values your privacy. By submitting your information, you are gaining access to C&EN and subscribing to our weekly newsletter. We use the information you provide to make your reading experience better, and we will never sell your data to third party members.

ENJOY UNLIMITED ACCES TO C&EN

Biological Chemistry

Key Measles Protein Revealed

November 26, 2007 | A version of this story appeared in Volume 85, Issue 48

The structure of a key protein found on the surface of the measles virus could help researchers identify an effective treatment for the disease, according to K. Christopher Garcia and coworkers at Stanford University School of Medicine (Nat. Struct. Mol. Biol., DOI: 10.1038/nsmb1342). Measles, which is characterized by fever and a rash, affects some 20 million people worldwide each year. Although there is an effective measles vaccine, not everybody receives it, and there is no drug treatment for those who contract the disease. Garcia and coworkers report the first crystal structure of measles virus hemagglutinin (shown, with glycan groups in gray). This is the surface glycoprotein that the virus uses to bind to host receptors when it infects cells. The work reveals that the propeller-shaped protein is structurally similar to neuraminidase enzymes that other viruses, such as influenza, use to infect host cells. It doesn't have neuraminidase's usual enzymatic activity, however, making it a "dead" neuraminidase. "Our structure now provides a template for structure-based drug design aimed at blocking measles virus entry," the researchers write.

Article:

This article has been sent to the following recipient:

0 /1 FREE ARTICLES LEFT THIS MONTH Remaining
Chemistry matters. Join us to get the news you need.