title: Effect of Ebola virus proteins GP, NP and VP35 on VP40 VLP morphology.
abstract: Recently we described a role for Ebola virus proteins, NP, GP, and VP35 in enhancement of VP40 VLP budding. To explore the possibility that VLP structure was altered by co-expression of EBOV proteins leading to the observed enhancement of VP40 VLP budding, we performed density gradient analysis as well as electron microscopy studies. Our data suggest that VP40 is the major determinant of VLP morphology, as co-expression of NP, GP and VP35 did not significantly change VLP density, length, and diameter. Ultra-structural changes were noted in the core of the VLPs when NP was co-expressed with VP40. Overall, these findings indicate that major changes in morphology of VP40 VLPs were likely not responsible for enhanced budding of VP40 VLPs in the presence of GP, NP and/or VP35.
authors.affiliation: Department of Pathobiology, School of Veterinary Medicine, University of Pennsylvania, 3800 Spruce St,, Philadelphia, PA 19104, USA. rfj@vet.upenn.edu
authors.forename: Reed F
authors.initials: RF
authors.lastname: Johnson
authors.forename: Peter
authors.initials: P
authors.lastname: Bell
authors.forename: Ronald N
authors.initials: RN
authors.lastname: Harty
mesh_terms: D002460:Cell Line; D029043:Ebolavirus / Q000648:ultrastructure*; D006801:Humans; D008854:Microscopy, Electron; D019590:Nucleocapsid Proteins / Q000502:physiology*; D009698:Nucleoproteins / Q000502:physiology*; D014758:Viral Core Proteins / Q000502:physiology*; D014759:Viral Envelope Proteins / Q000502:physiology*; D014771:Virion / Q000648:ultrastructure*; D019065:Virus Assembly
chemical_list: D019590:Nucleocapsid Proteins; D009698:Nucleoproteins; D014758:Viral Core Proteins; D014759:Viral Envelope Proteins; C113189:envelope glycoprotein, Ebola virus; C084818:nucleoprotein VP35, Ebola virus; C084819:nucleoprotein VP40, Ebola virus