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Your search keyword '"Infection Biology Research Program"' showing total 2 results
Start Over Author "Infection Biology Research Program" Publisher elsevier science
2 results on '"Infection Biology Research Program"'

1. Mutational analysis of positively charged amino acid residues of Uukuniemi phlebovirus nucleocapsid protein.

Author

Katz A, Freiberg AN, Backström V, Holm L, Vaheri A, Flick R, and Plyusnin A

Subjects
Amino Acid Sequence, Amino Acids chemistry, Amino Acids genetics, Amino Acids metabolism, DNA Mutational Analysis, Molecular Sequence Data, Nucleocapsid Proteins chemistry, Nucleocapsid Proteins metabolism, Phlebovirus chemistry, Phlebovirus genetics, Phlebovirus metabolism, Sequence Alignment, Uukuniemi virus chemistry, Uukuniemi virus metabolism, Mutation, Nucleocapsid Proteins genetics, Uukuniemi virus genetics
Abstract

The aim of this study was to evaluate the contribution of positively charged amino acid residues for the Uukuniemi virus (UUKV) N protein functionality. Based on phlebovirus nucleocapsid (N) protein alignments and 3D-structure predictions of UUKV N protein, 14 positively charged residues were chosen as targets for the mutagenesis. The impact of mutations to the N protein functionality was analyzed using minigenome-, virus-like particle-, and mammalian two-hybrid-assays. Seven of the mutations affected the functional competence in all three assays, while others had milder impact or no impact at all. In the 3D-model of UUKV N protein, five of the affected residues, R61, R64, R73, R98 and R115, were located either within or in close proximity to the central cavity that could potentially bind RNA.

Published
2012
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2. Interaction between hantaviral nucleocapsid protein and the cytoplasmic tail of surface glycoprotein Gn.

Author

Wang H, Alminaite A, Vaheri A, and Plyusnin A

Subjects
Amino Acid Sequence, Cell Line, Humans, Membrane Glycoproteins chemistry, Membrane Glycoproteins genetics, Models, Molecular, Molecular Sequence Data, Nucleocapsid Proteins genetics, Protein Binding, Protein Structure, Tertiary, Sequence Alignment, Orthohantavirus physiology, Membrane Glycoproteins metabolism, Nucleocapsid Proteins metabolism, Protein Interaction Domains and Motifs, Protein Interaction Mapping, Viral Proteins metabolism
Abstract

Hantaviral N and Gn proteins were shown to interact, thus providing the long-awaited evidence for one of the crucial steps in the virus replication at which RNPs are directed to the site of the virus assembly. Using pull-down assay and point mutagenesis it was demonstrated that intact, properly folded zinc fingers in the Gn protein cytoplasmic tail as well as the middle domain of the N protein (that includes aa residues 80-248) are essential for the interaction., (Copyright 2010 Elsevier B.V. All rights reserved.)

Published
2010
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