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Lipid binding properties of Ebola virus matrix protein VP40
Author(s) -
Yong Sylvia,
Scott Jordan L.,
Stahelin Robert V.
Publication year - 2013
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.27.1_supplement.1021.9
Subject(s) - ebola virus , vp40 , ebolavirus , virology , phosphatidylserine , viral matrix protein , secretion , biology , virus , microbiology and biotechnology , chemistry , phospholipid , biochemistry , membrane
The Ebola virus (EBOV) is a pathogen that causes hemorrhagic fevers in humans. It is most prevalent in Africa, where outbreaks with fatality rates of up to 90% have occurred. It also poses a global threat as infections can be spread rapidly. While it is known that EBOV infections function by inhibiting the immune system, the specific cellular secretion pathway of the virus has not been uncovered. As no treatment for this deadly virus exists, it is important to learn how EBOV co‐opts infected cells in order to pharmacologically target the formation and egress of new virions. VP40, one of the seven structural proteins that EBOV encodes, is essential for initiation of new virion formation at the plasma membrane. In this study, vesicular sedimentation assays were used to better understand the lipid binding properties of VP40. In addition, surface plamon resonance (SPR) was used to determine the binding specificity of the wild type VP40 and mutant VP40 A299W. VP40 WT and VP40 A299W bind phosphatidylserine (PS), a plasma membrane phospholipid, with equal affinity. VP40 is essential for EBOV cellular egress and the mechanisms by which it is targeted to the plasma membrane and subsequently recruits the virus capsid are under further investigation. This research is supported by the NIH (AI081077).