Characterization of N protein self-association in coronavirus ribonucleoprotein complexes

Krishna Narayanan, Kyongmin Hwang Kim, Shinji Makino

Research output: Contribution to journalArticle

33 Citations (Scopus)

Abstract

Mouse hepatitis virus (MHV) nucleocapsid (N) protein binds to the large, single-stranded, positive-sense viral genomic RNA to form a helical nucleocapsid structure in mature virions. In addition N protein binds the intracellular form of the genomic RNA, all of the MHV subgenomic mRNAs, and expressed non-MHV RNA transcripts to form ribonucleoprotein (RNP) complexes in infected cells. Among the intracellular viral RNP complexes, only the genomic RNP complex is packaged into virus particles. The present study demonstrated that N protein in the MHV virion nucleocapsid and in the intracellular genome-length RNP complex that bound to viral envelope M protein was tightly self-associated such that its association was retained even after extensive RNase A-treatment of the RNP complexes. The RNase A-resistant tight N protein association in the virion nucleocapsid was not mediated by an intermolecular disulfide bridge between N proteins. In contrast, N protein association in the majority of the intracellular RNP complexes was susceptible to RNase A-treatment. Because the RNP complexes that specifically interact with the M protein are selectively packaged into MHV particles, the present data suggested that there was a distinct difference between N protein association in viral genomic RNP complexes that undergo packaging into virus particles and the subgenomic RNP complexes that are not packaged into MHV particles.

Original languageEnglish (US)
Pages (from-to)131-140
Number of pages10
JournalVirus Research
Volume98
Issue number2
DOIs
StatePublished - Dec 2003

Fingerprint

Coronavirus
Ribonucleoproteins
Virion
Murine hepatitis virus
Nucleocapsid
Pancreatic Ribonuclease
Proteins
Viral Matrix Proteins
RNA
Viral Envelope Proteins
Hepatitis Viruses
Viral RNA
Product Packaging
Disulfides
Genome
Messenger RNA

Keywords

  • Coronavirus
  • N protein
  • Ribonucleoprotein (RNP) complexes

ASJC Scopus subject areas

  • Cancer Research
  • Molecular Biology
  • Virology

Cite this

Characterization of N protein self-association in coronavirus ribonucleoprotein complexes. / Narayanan, Krishna; Kim, Kyongmin Hwang; Makino, Shinji.

In: Virus Research, Vol. 98, No. 2, 12.2003, p. 131-140.

Research output: Contribution to journalArticle

Narayanan, Krishna ; Kim, Kyongmin Hwang ; Makino, Shinji. / Characterization of N protein self-association in coronavirus ribonucleoprotein complexes. In: Virus Research. 2003 ; Vol. 98, No. 2. pp. 131-140.
@article{d5d1544e9e1c466baa5dec3576d40266,
title = "Characterization of N protein self-association in coronavirus ribonucleoprotein complexes",
abstract = "Mouse hepatitis virus (MHV) nucleocapsid (N) protein binds to the large, single-stranded, positive-sense viral genomic RNA to form a helical nucleocapsid structure in mature virions. In addition N protein binds the intracellular form of the genomic RNA, all of the MHV subgenomic mRNAs, and expressed non-MHV RNA transcripts to form ribonucleoprotein (RNP) complexes in infected cells. Among the intracellular viral RNP complexes, only the genomic RNP complex is packaged into virus particles. The present study demonstrated that N protein in the MHV virion nucleocapsid and in the intracellular genome-length RNP complex that bound to viral envelope M protein was tightly self-associated such that its association was retained even after extensive RNase A-treatment of the RNP complexes. The RNase A-resistant tight N protein association in the virion nucleocapsid was not mediated by an intermolecular disulfide bridge between N proteins. In contrast, N protein association in the majority of the intracellular RNP complexes was susceptible to RNase A-treatment. Because the RNP complexes that specifically interact with the M protein are selectively packaged into MHV particles, the present data suggested that there was a distinct difference between N protein association in viral genomic RNP complexes that undergo packaging into virus particles and the subgenomic RNP complexes that are not packaged into MHV particles.",
keywords = "Coronavirus, N protein, Ribonucleoprotein (RNP) complexes",
author = "Krishna Narayanan and Kim, {Kyongmin Hwang} and Shinji Makino",
year = "2003",
month = "12",
doi = "10.1016/j.virusres.2003.08.021",
language = "English (US)",
volume = "98",
pages = "131--140",
journal = "Virus Research",
issn = "0168-1702",
publisher = "Elsevier",
number = "2",

}

TY - JOUR

T1 - Characterization of N protein self-association in coronavirus ribonucleoprotein complexes

AU - Narayanan, Krishna

AU - Kim, Kyongmin Hwang

AU - Makino, Shinji

PY - 2003/12

Y1 - 2003/12

N2 - Mouse hepatitis virus (MHV) nucleocapsid (N) protein binds to the large, single-stranded, positive-sense viral genomic RNA to form a helical nucleocapsid structure in mature virions. In addition N protein binds the intracellular form of the genomic RNA, all of the MHV subgenomic mRNAs, and expressed non-MHV RNA transcripts to form ribonucleoprotein (RNP) complexes in infected cells. Among the intracellular viral RNP complexes, only the genomic RNP complex is packaged into virus particles. The present study demonstrated that N protein in the MHV virion nucleocapsid and in the intracellular genome-length RNP complex that bound to viral envelope M protein was tightly self-associated such that its association was retained even after extensive RNase A-treatment of the RNP complexes. The RNase A-resistant tight N protein association in the virion nucleocapsid was not mediated by an intermolecular disulfide bridge between N proteins. In contrast, N protein association in the majority of the intracellular RNP complexes was susceptible to RNase A-treatment. Because the RNP complexes that specifically interact with the M protein are selectively packaged into MHV particles, the present data suggested that there was a distinct difference between N protein association in viral genomic RNP complexes that undergo packaging into virus particles and the subgenomic RNP complexes that are not packaged into MHV particles.

AB - Mouse hepatitis virus (MHV) nucleocapsid (N) protein binds to the large, single-stranded, positive-sense viral genomic RNA to form a helical nucleocapsid structure in mature virions. In addition N protein binds the intracellular form of the genomic RNA, all of the MHV subgenomic mRNAs, and expressed non-MHV RNA transcripts to form ribonucleoprotein (RNP) complexes in infected cells. Among the intracellular viral RNP complexes, only the genomic RNP complex is packaged into virus particles. The present study demonstrated that N protein in the MHV virion nucleocapsid and in the intracellular genome-length RNP complex that bound to viral envelope M protein was tightly self-associated such that its association was retained even after extensive RNase A-treatment of the RNP complexes. The RNase A-resistant tight N protein association in the virion nucleocapsid was not mediated by an intermolecular disulfide bridge between N proteins. In contrast, N protein association in the majority of the intracellular RNP complexes was susceptible to RNase A-treatment. Because the RNP complexes that specifically interact with the M protein are selectively packaged into MHV particles, the present data suggested that there was a distinct difference between N protein association in viral genomic RNP complexes that undergo packaging into virus particles and the subgenomic RNP complexes that are not packaged into MHV particles.

KW - Coronavirus

KW - N protein

KW - Ribonucleoprotein (RNP) complexes

UR - http://www.scopus.com/inward/record.url?scp=0345490757&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0345490757&partnerID=8YFLogxK

U2 - 10.1016/j.virusres.2003.08.021

DO - 10.1016/j.virusres.2003.08.021

M3 - Article

C2 - 14659560

AN - SCOPUS:0345490757

VL - 98

SP - 131

EP - 140

JO - Virus Research

JF - Virus Research

SN - 0168-1702

IS - 2

ER -