原创力文档bkv agnoprotein interacts with α-soluble n-ethylmaleimide-sensitive fusion attachment protein, and negatively influences transport of vsvg-egfpbkv agnoprotein与α-soluble n-ethylmaleimide-sensitive融合附件蛋白质,和负面影响vsvg-egfp运输.pdfVIP
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bkv agnoprotein interacts with α-soluble n-ethylmaleimide-sensitive fusion attachment protein, and negatively influences transport of vsvg-egfpbkv agnoprotein与α-soluble n-ethylmaleimide-sensitive融合附件蛋白质,和负面影响vsvg-egfp运输
BKV Agnoprotein Interacts with a-Soluble
N-Ethylmaleimide-Sensitive Fusion Attachment Protein,
and Negatively Influences Transport of VSVG-EGFP
1 1 1 1 2 1
Mona Johannessen *, Mari Walquist , Nancy Gerits , Marte Dragset , Anne Spang , Ugo Moens
1 Research Group of Host-Microbe Interactions, Department of Medical Biology, Faculty of Health Sciences, University of Tromsø, Tromsø, Norway, 2 Biozentrum,
University of Basel, Basel, Switzerland
Abstract
Background: The human polyomavirus BK (BKV) infects humans worldwide and establishes a persistent infection in the
kidney. The BK virus genome encodes three regulatory proteins, large and small tumor-antigen and the agnoprotein, as well
as the capsid proteins VP1 to VP3. Agnoprotein is conserved among BKV, JC virus (JCV) and SV40, and agnoprotein-deficient
mutants reveal reduced viral propagation. Studies with JCV and SV40 indicate that their agnoproteins may be involved in
transcription, replication and/or nuclear and cellular release of the virus. However, the exact function(s) of agnoprotein of BK
virus remains elusive.
Principal Findings: As a strategy of exploring the functions of BKV agnoprotein, we decided to look for cellular interaction
partners for the viral protein. Several partners were identified by yeast two-hybrid assay, among them a-SNAP which is
involved in disassembly of vesicles during secretion. BKV agnoprotein and a-SNAP were found to partially co-localize in cells,
and a complex consisting of agnoprotein and a-SNAP could be co-immunoprecipitated from cells ectopically expressing the
proteins as well as from BKV-transfected cells. The N-terminal part of the agnoprotein was sufficient for the interaction with
a-SNAP. Finally, we c
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