Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
6142915 | Virus Research | 2013 | 4 Pages |
Abstract
Among the herpesvirus glycoprotein B (gB) fusion proteins, the hydrophobic content of fusion loops and membrane proximal regions (MPRs) are inversely correlated with each other. We examined the functional importance of the hydrophobicity of these regions by replacing them in herpes simplex virus type 1 gB with corresponding regions from Epstein-Barr virus gB. We show that fusion activity is dependent on the structural context in which the specific loops and MPR sequences exist, rather than a simple hydrophobic relationship.
Related Topics
Life Sciences
Immunology and Microbiology
Virology
Authors
Anna Zago, Sarah A. Connolly, Patricia G. Spear, Richard Longnecker,