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  Characterization of host proteins interacting with the lymphocytic choriomeningitis virus L protein

Khamina, K., Lercher, A., Caldera, M., Schliehe, C., Vilagos, B., Sahin, M., et al. (2017). Characterization of host proteins interacting with the lymphocytic choriomeningitis virus L protein. PLoS Pathogens, 13(12): e1006758. doi:10.1371/journal.ppat.1006758.

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Item Permalink: http://hdl.handle.net/21.11116/0000-0000-739C-F Version Permalink: http://hdl.handle.net/21.11116/0000-0000-739D-E
Genre: Journal Article

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 Creators:
Khamina, Kseniya1, Author
Lercher, Alexander1, Author
Caldera, Michael1, Author
Schliehe, Christopher1, Author
Vilagos, Bojan1, Author
Sahin, Mehmet1, Author
Kosack, Lindsay1, Author
Bhattacharya, Anannya1, Author
Majek, Peter1, Author
Stukalov, Alexey2, Author              
Sacco, Roberto1, Author
James, Leo C.1, Author
Pinschewer, Daniel D.1, Author
Bennett, Keiryn L.1, Author
Menche, Jorg1, Author
Bergthaler, Andreas1, Author
Affiliations:
1external, ou_persistent22              
2Pichlmair, Andreas / Innate Immunity, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565166              

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Free keywords: MASS-SPECTROMETRY DATA; VIRAL-RNA SYNTHESIS; RECEPTOR TRIM21; I INTERFERON; INFECTION; IDENTIFICATION; PERSISTENCE; PROTEOMICS; INFLUENZA; SOFTWAREMicrobiology; Parasitology; Virology;
 Abstract: RNA-dependent RNA polymerases (RdRps) play a key role in the life cycle of RNA viruses and impact their immunobiology. The arenavirus lymphocytic choriomeningitis virus (LCMV) strain Clone 13 provides a benchmark model for studying chronic infection. A major genetic determinant for its ability to persist maps to a single amino acid exchange in the viral L protein, which exhibits RdRp activity, yet its functional consequences remain elusive. To unravel the L protein interactions with the host proteome, we engineered infectious L protein-tagged LCMV virions by reverse genetics. A subsequent mass-spectrometric analysis of L protein pulldowns from infected human cells revealed a comprehensive network of interacting host proteins. The obtained LCMV L protein interactome was bioinformatically integrated with known host protein interactors of RdRps from other RNA viruses, emphasizing interconnected modules of human proteins. Functional characterization of selected interactors highlighted proviral (DDX3X) as well as antiviral (NKRF, TRIM21) host factors. To corroborate these findings, we infected Trim21(-/-) mice with LCMV and found impaired virus control in chronic infection. These results provide insights into the complex interactions of the arenavirus LCMV and other viral RdRps with the host proteome and contribute to a better molecular understanding of how chronic viruses interact with their host.

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Language(s): eng - English
 Dates: 2017-12-20
 Publication Status: Published online
 Pages: 20
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 Table of Contents: -
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Title: PLoS Pathogens
  Other : PLoS Pathog.
Source Genre: Journal
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Publ. Info: San Francisco, CA : Public Library of Science
Pages: - Volume / Issue: 13 (12) Sequence Number: e1006758 Start / End Page: - Identifier: ISSN: 1553-7366
CoNE: https://pure.mpg.de/cone/journals/resource/1000000000018830