Effect of Ebola virus proteins GP, NP and VP35 on VP40VLP morphology

被引:66
作者
Johnson, Reed F.
Bell, Peter
Harty, Ronald N.
机构
[1] Univ Penn, Sch Vet Med, Dept Pathobiol, Philadelphia, PA 19104 USA
[2] Univ Penn, Sch Med, Dept Pathol & Lab Med, Gene Therapy Program, Philadelphia, PA 19104 USA
关键词
D O I
10.1186/1743-422X-3-31
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
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.
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页数:7
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