Cross-species analysis of the replication complex of Old World arenaviruses reveals two nucleoprotein sites involved in L protein function.

Détails

ID Serval
serval:BIB_DD76504265B9
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Institution
Titre
Cross-species analysis of the replication complex of Old World arenaviruses reveals two nucleoprotein sites involved in L protein function.
Périodique
Journal of Virology
Auteur⸱e⸱s
Kerber R., Rieger T., Busch C., Flatz L., Pinschewer D.D., Kümmerer B.M., Günther S.
ISSN
1098-5514 (Electronic)
ISSN-L
0022-538X
Statut éditorial
Publié
Date de publication
2011
Volume
85
Numéro
23
Pages
12518-12528
Langue
anglais
Notes
Publication types: Journal Article ; Research Support, Non-U.S. Gov'tPublication Status: ppublish
Résumé
Lassa virus (LASV) causing hemorrhagic Lassa fever in West Africa, Mopeia virus (MOPV) from East Africa, and lymphocytic choriomeningitis virus (LCMV) are the main representatives of the Old World arenaviruses. Little is known about how the components of the arenavirus replication machinery, i.e., the genome, nucleoprotein (NP), and L protein, interact. In addition, it is unknown whether these components can function across species boundaries. We established minireplicon systems for MOPV and LCMV in analogy to the existing LASV system and exchanged the components among the three systems. The functional and physical integrity of the resulting complexes was tested by reporter gene assay, Northern blotting, and coimmunoprecipitation studies. The minigenomes, NPs, and L proteins of LASV and MOPV could be exchanged without loss of function. LASV and MOPV L protein was also active in conjunction with LCMV NP, while the LCMV L protein required homologous NP for activity. Analysis of LASV/LCMV NP chimeras identified a single LCMV-specific NP residue (Ile-53) and the C terminus of NP (residues 340 to 558) as being essential for LCMV L protein function. The defect of LASV and MOPV NP in supporting transcriptional activity of LCMV L protein was not caused by a defect in physical NP-L protein interaction. In conclusion, components of the replication complex of Old World arenaviruses have the potential to functionally and physically interact across species boundaries. Residue 53 and the C-terminal domain of NP are important for function of L protein during genome replication and transcription.
Mots-clé
Amino Acid Sequence, Animals, Arenaviridae Infections/genetics, Arenaviridae Infections/metabolism, Arenaviruses, Old World/classification, Arenaviruses, Old World/genetics, Blotting, Northern, Blotting, Western, Cercopithecus aethiops, DNA Replication, DNA, Viral/genetics, Immunoprecipitation, Molecular Sequence Data, Nucleoproteins/genetics, Nucleoproteins/metabolism, RNA, Viral/genetics, Regulatory Elements, Transcriptional, Replicon/genetics, Sequence Homology, Amino Acid, Species Specificity, Transcriptional Activation, Vero Cells, Viral Proteins/genetics, Viral Proteins/metabolism
Pubmed
Web of science
Open Access
Oui
Création de la notice
23/03/2012 18:03
Dernière modification de la notice
20/08/2019 16:02
Données d'usage