Publications by authors named "Helen K McPhee"
The propensity of a matrix protein from an enveloped virus of the Mononegavirales family to associate with lipids representative of the viral envelope has been determined using label-free methods, including tensiometry and Brewster angle microscopy on lipid films at the air-water interface and atomic force microscopy on monolayers transferred to OTS-treated silicon wafers. This has enabled factors that influence the disposition of the protein with respect to the lipid interface to be characterized. In the absence of sphingomyelin, respiratory syncytial virus matrix protein penetrates monolayers composed of mixtures of phosphocholines with phosphoethanolamines or cholesterol at the air-water interface.
View Article and Find Full Text PDFArticle Synopsis
- The matrix protein (M) of respiratory syncytial virus (RSV) has been crystallized, revealing its structure with two compact beta-rich domains linked by a less structured area.
- The protein features a large positive surface charge area, facilitating interactions with negatively charged membranes or other viral components.
- Differences in the RSV M sequence compared to other Pneumovirinae viruses are mainly found in surface-exposed loops, particularly in the N-terminal domain.