Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.

Science 14 July 2006:
Vol. 313. no. 5784, p. 144
DOI: 10.1126/science.313.5784.144j
Prev | Table of Contents | Next

This Week in Science

Figure 1 Enveloped viruses deliver their genome into the host by fusing with its membrane. Two classes of viral glycoproteins that drive membrane fusion through conformational changes have been identified, but a number of viral fusion proteins do not fall into either of these classes. Roche et al. (p. 187) have determined the crystal structure of the atypical membrane fusion glycoprotein (G) from vesicular stomatitis virus, and Heldwein et al. (p. 217) have determined the structure of glycoprotein B (gB), a conserved component of the complex cell entry machinery of herpes simplex virus (HSV-1). Unexpectedly, G and gB are homologous with both combining features of fusion proteins from classes I and II. This homology identifies gB as the viral fusogen in HSV-1 and has interesting implications in considering the evolution of viral fusion proteins (see the Perspective by Steven and Spear).

CREDIT: ROCHE ET AL.




To Advertise     Find Products

Science. ISSN 0036-8075 (print), 1095-9203 (online)