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

Anna Katz, Alexander Freiberg, Vera Backström, Liisa Holm, Antti Vaheri, Ramon Flick, Alexander Plyusnin

Research output: Contribution to journalArticle

1 Citation (Scopus)

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.

Original languageEnglish (US)
Pages (from-to)118-123
Number of pages6
JournalVirus Research
Volume167
Issue number1
DOIs
StatePublished - Jul 2012

Fingerprint

Phlebovirus
Uukuniemi virus
Nucleocapsid Proteins
Amino Acids
Proteins
Two-Hybrid System Techniques
Mutation
Mutagenesis
Virion
Mental Competency
RNA

Keywords

  • Mutational analysis
  • Negative-strand RNA virus
  • Nucleocapsid protein
  • Oligomerization
  • Phlebovirus
  • RNA binding
  • Uukuniemi virus

ASJC Scopus subject areas

  • Virology
  • Infectious Diseases
  • Cancer Research

Cite this

Mutational analysis of positively charged amino acid residues of Uukuniemi phlebovirus nucleocapsid protein. / Katz, Anna; Freiberg, Alexander; Backström, Vera; Holm, Liisa; Vaheri, Antti; Flick, Ramon; Plyusnin, Alexander.

In: Virus Research, Vol. 167, No. 1, 07.2012, p. 118-123.

Research output: Contribution to journalArticle

Katz, Anna ; Freiberg, Alexander ; Backström, Vera ; Holm, Liisa ; Vaheri, Antti ; Flick, Ramon ; Plyusnin, Alexander. / Mutational analysis of positively charged amino acid residues of Uukuniemi phlebovirus nucleocapsid protein. In: Virus Research. 2012 ; Vol. 167, No. 1. pp. 118-123.
@article{87379e45ebee4c31a08563f8a1f94fb0,
title = "Mutational analysis of positively charged amino acid residues of Uukuniemi phlebovirus nucleocapsid protein",
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.",
keywords = "Mutational analysis, Negative-strand RNA virus, Nucleocapsid protein, Oligomerization, Phlebovirus, RNA binding, Uukuniemi virus",
author = "Anna Katz and Alexander Freiberg and Vera Backstr{\"o}m and Liisa Holm and Antti Vaheri and Ramon Flick and Alexander Plyusnin",
year = "2012",
month = "7",
doi = "10.1016/j.virusres.2012.04.003",
language = "English (US)",
volume = "167",
pages = "118--123",
journal = "Virus Research",
issn = "0168-1702",
publisher = "Elsevier",
number = "1",

}

TY - JOUR

T1 - Mutational analysis of positively charged amino acid residues of Uukuniemi phlebovirus nucleocapsid protein

AU - Katz, Anna

AU - Freiberg, Alexander

AU - Backström, Vera

AU - Holm, Liisa

AU - Vaheri, Antti

AU - Flick, Ramon

AU - Plyusnin, Alexander

PY - 2012/7

Y1 - 2012/7

N2 - 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.

AB - 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.

KW - Mutational analysis

KW - Negative-strand RNA virus

KW - Nucleocapsid protein

KW - Oligomerization

KW - Phlebovirus

KW - RNA binding

KW - Uukuniemi virus

UR - http://www.scopus.com/inward/record.url?scp=84861482042&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84861482042&partnerID=8YFLogxK

U2 - 10.1016/j.virusres.2012.04.003

DO - 10.1016/j.virusres.2012.04.003

M3 - Article

C2 - 22808531

AN - SCOPUS:84861482042

VL - 167

SP - 118

EP - 123

JO - Virus Research

JF - Virus Research

SN - 0168-1702

IS - 1

ER -