Effect of Ebola virus proteins GP, NP and VP35 on VP40 VLP morphology.docVIP

Virology Journal BioMedCentral Research Open Access Effect of Ebola virus proteins GP, NP and VP35 on VP40 VLP morphology Reed F Johnson1, Peter Bell2 and Ronald N Harty*1 Address: 1Department of Pathobiology, School of Veterinary Medicine, University of Pennsylvania, 3800 Spruce St., Philadelphia, PA 19104, USA and 2Gene Therapy Program, Department of Pathology and Laboratory Medicine, School of Medicine, University of Pennsylvania, Philadelphia, PA 19104, USA Email: Reed F Johnson - rfj@; Peter Bell - pbell@; Ronald N Harty* - rharty@ * Corresponding author Published: 23 May 2006 Received: 26 April 2006 Accepted: 23 May 2006 Virology Journal 2006, 3:31 doi:10.1186/1743-422X-3-31 This article is available from: /content/3/1/31 ? 2006 Johnson et al; licensee BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. 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. Introduction into the mechanisms of VP40 VLP budding will lead to possible vaccines and therapeutics t