Year: 2015
Type: article
Abstract: The crystal structure of the F protein (prefusion form) of the paramyxovirus parainfluenza virus 5 (PIV5) WR isolate was determined. We investigated the basis by which point mutations affect fusion in PIV5 isolates W3A and WR, which differ by two residues in the F ectodomain. The P22 stabilizing site acts through a local conformational change and a hydrophobic pocket interaction, whereas the S443 destabilizing site appears sensitive to both conformational effects and amino acid charge/polarity changes.
Source: Journal of Virology
DOI: 10.1128/jvi.03221-14
Language: English
Topic: Virology and Viral Diseases
Subfield: Epidemiology
Field: Medicine
Domain: Health Sciences
Open Access status: bronze
Funders: Howard Hughes Medical Institute, U.S. Department of Energy, National Institutes of Health, Office of Science, Michigan Technology Tri-Corridor, National Cancer Institute, National Institute of General Medical Sciences, National Institute of Allergy and Infectious Diseases, Basic Energy Sciences
Awards: G1266841304, G1286251239, G191313393, Medical Scientist Training Program, Structural Studies of Paramyxovirus fusion proteins, G498139845, MONet Test Samples for Analytics, Structure and Expression of the Paramyxovirus SV5 Genome, The Robert H. Lurie Comprehensive Cancer Center, G969889393, G997124007
OpenAlex ID: W2010091989