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Citation link: http://nbn-resolving.de/urn:nbn:de:gbv:46-00103254-15
00103254-1.pdf
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Expression und Charakterisierung des Andes-Virus L-Proteins


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Other Titles: Expression and characterization of the Andes virus L protein
Authors: Heinemann, Patrick 
Supervisor: Schmidt-Chanasit, Jonas 
1. Expert: Dotzauer, Andreas
2. Expert: Günther, Stephan
Abstract: 
Andes virus (ANDV) is a member of the genus Hantavirus. Little is known about structure and function of the hantaviral L protein. Sequence alignments revealed a putative RNA-dependent RNA polymerase domain in the center and an endonuclease at the N terminus. Studying hantaviral L proteins is difficult, because recombinant L protein expression in mammalian cells is very ineffective. Deletion analysis revealed that the N terminus determine the low-expression phenotype. This work demonstrates that ANDV L protein expression can be rescued upon mutation of catalytic amino acids and further conserved residues of the putative endonuclease domain. In addition, wild-type ANDV L rather than expressible L mutants suppressed the level of mRNA and reduces protein expression. Expressible ANDV L mutants colocalized with the cellular processing (P) bodies, ANDV N and NSs protein, but not with the glycoprotein Gc. This work suggests that ANDV L protein possesses an endonuclease at the N terminus suppressing the level of its own as well as heterologous mRNAs upon recombinant expression in mammalian cells.
Keywords: Hantavirus, polymerase, L protein, endonuclease
Issue Date: 31-May-2013
Type: Dissertation
URN: urn:nbn:de:gbv:46-00103254-15
Institution: Universität Bremen 
Faculty: FB2 Biologie/Chemie 
Appears in Collections:Dissertationen

  

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