Structural model of the pre-pore ring-like structure of Panton-Valentine leukocidin: providing dimensionality to biophysical and mutational data.
Panton-Valentine leukocidin (PVL) is a bipartite toxin that plays an important role in the pathogenesis of methicillin-resistant Staphylococcus aureus. Recent clinical data suggest a correlation between PVL and severe cases of S. aureus pneumonia. A clear understanding of the structure and function of PVL is critical to the development of novel, effective treatments. Here, we report an all-atom model of the macromolecular structure of Panton-Valentine leukocidin in its octameric, pre-pore conformation that confirms and extends our understanding of the toxin's mechanism of action.
Aman
M Javad
MJ
Integrated BioTherapeutics, Inc., Germantown, MD 20876, USA. nguyent5@mail.nih.gov
Karauzum
Hatice
H
Bowden
M Gabriela
MG
Nguyen
Tam Luong
TL
D001427:Bacterial Toxins / Q000737:chemistry* / Q000235:genetics; D018360:Crystallography, X-Ray; D005098:Exotoxins / Q000737:chemistry* / Q000235:genetics; D006801:Humans; D006860:Hydrogen Bonding; D007956:Leukocidins / Q000737:chemistry* / Q000235:genetics; D055624:Methicillin-Resistant Staphylococcus aureus / Q000737:chemistry*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009154:Mutation; D011487:Protein Conformation
D001427:Bacterial Toxins; D005098:Exotoxins; D007956:Leukocidins; C078284:Panton-Valentine leukocidin