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The L-VP35 and L-L interaction domains reside in the amino terminus of the Ebola virus L protein and are potential targets for antivirals.

Trunschke, Martina ; Conrad, Dominik ; Enterlein, Sven ; Olejnik, Judith ; Brauburger, Kristina LU and Mühlberger, Elke (2013) In Virology 441(2). p.135-145
Abstract
The Ebola virus (EBOV) RNA-dependent RNA polymerase (RdRp) complex consists of the catalytic subunit of the polymerase, L, and its cofactor VP35. Using immunofluorescence analysis and coimmunoprecipitation assays, we mapped the VP35 binding site on L. A core binding domain spanning amino acids 280-370 of L was sufficient to mediate weak interaction with VP35, while the entire N-terminus up to amino acid 380 was required for strong VP35-L binding. Interestingly, the VP35 binding site overlaps with an N-terminal L homo-oligomerization domain in a non-competitive manner. N-terminal L deletion mutants containing the VP35 binding site were able to efficiently block EBOV replication and transcription in a minigenome system suggesting the VP35... (More)
The Ebola virus (EBOV) RNA-dependent RNA polymerase (RdRp) complex consists of the catalytic subunit of the polymerase, L, and its cofactor VP35. Using immunofluorescence analysis and coimmunoprecipitation assays, we mapped the VP35 binding site on L. A core binding domain spanning amino acids 280-370 of L was sufficient to mediate weak interaction with VP35, while the entire N-terminus up to amino acid 380 was required for strong VP35-L binding. Interestingly, the VP35 binding site overlaps with an N-terminal L homo-oligomerization domain in a non-competitive manner. N-terminal L deletion mutants containing the VP35 binding site were able to efficiently block EBOV replication and transcription in a minigenome system suggesting the VP35 binding site on L as a potential target for the development of antivirals. (Less)
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author
publishing date
type
Contribution to journal
publication status
published
subject
in
Virology
volume
441
issue
2
pages
135 - 145
publisher
Elsevier
external identifiers
  • scopus:84877920406
  • pmid:23582637
ISSN
1096-0341
DOI
10.1016/j.virol.2013.03.013
language
English
LU publication?
no
id
f5db31e6-3b42-4235-a261-00416dbb640b (old id 8726488)
alternative location
http://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=23582637&retmode=ref&cmd=prlinks
date added to LUP
2016-04-01 13:21:10
date last changed
2020-01-12 12:00:39
@article{f5db31e6-3b42-4235-a261-00416dbb640b,
  abstract     = {The Ebola virus (EBOV) RNA-dependent RNA polymerase (RdRp) complex consists of the catalytic subunit of the polymerase, L, and its cofactor VP35. Using immunofluorescence analysis and coimmunoprecipitation assays, we mapped the VP35 binding site on L. A core binding domain spanning amino acids 280-370 of L was sufficient to mediate weak interaction with VP35, while the entire N-terminus up to amino acid 380 was required for strong VP35-L binding. Interestingly, the VP35 binding site overlaps with an N-terminal L homo-oligomerization domain in a non-competitive manner. N-terminal L deletion mutants containing the VP35 binding site were able to efficiently block EBOV replication and transcription in a minigenome system suggesting the VP35 binding site on L as a potential target for the development of antivirals.},
  author       = {Trunschke, Martina and Conrad, Dominik and Enterlein, Sven and Olejnik, Judith and Brauburger, Kristina and Mühlberger, Elke},
  issn         = {1096-0341},
  language     = {eng},
  number       = {2},
  pages        = {135--145},
  publisher    = {Elsevier},
  series       = {Virology},
  title        = {The L-VP35 and L-L interaction domains reside in the amino terminus of the Ebola virus L protein and are potential targets for antivirals.},
  url          = {http://dx.doi.org/10.1016/j.virol.2013.03.013},
  doi          = {10.1016/j.virol.2013.03.013},
  volume       = {441},
  year         = {2013},
}