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Severe acute respiratory syndrome coronavirus membrane protein interacts with nucleocapsid protein mostly through their carboxyl termini by electrostatic attraction.

Identifieur interne : 003D10 ( Main/Exploration ); précédent : 003D09; suivant : 003D11

Severe acute respiratory syndrome coronavirus membrane protein interacts with nucleocapsid protein mostly through their carboxyl termini by electrostatic attraction.

Auteurs : Haibin Luo [République populaire de Chine] ; Dalei Wu ; Can Shen ; Kaixian Chen ; Xu Shen ; Hualiang Jiang

Source :

The international journal of biochemistry & cell biology [ 1357-2725 ] ; 2006.

RBID : pubmed:16343974

Descripteurs français

English descriptors

KwdEn :
- Nucleocapsid Proteins (chemistry), Nucleocapsid Proteins (metabolism), Protein Binding, SARS Virus (chemistry), SARS Virus (metabolism), Static Electricity, Surface Plasmon Resonance, Viral Matrix Proteins (chemistry), Viral Matrix Proteins (metabolism), Virus Assembly.
MESH :
- chemical , chemistry : Nucleocapsid Proteins, Viral Matrix Proteins.
- chemical , metabolism : Nucleocapsid Proteins, Viral Matrix Proteins.
- chemistry : SARS Virus.
- metabolism : SARS Virus.
- Protein Binding, Static Electricity, Surface Plasmon Resonance, Virus Assembly.

Abstract

The severe acute respiratory syndrome coronavirus (SARS-CoV) membrane protein is an abundant virion protein, and its interaction with the nucleocapsid protein is crucial for viral assembly and morphogenesis. Although the interacting region in the nucleocapsid protein was mapped to residues 168-208, the interacting region in the membrane protein and the interaction nature are still unclear. In this work, by using yeast two-hybrid and surface plasmon resonance techniques, the residues 197-221 of the membrane protein and the residues 351-422 of the nucleocapsid protein were determined to be involved in their interaction. Sequence analysis revealed that these two fragments are highly charged at neutral pH, suggesting that their interaction may be of ionic nature. Kinetic assays indicated that the endodomain (aa102-221) of the membrane protein interacts with the nucleocapsid protein with high affinity (K(D)=0.55+/-0.04 microM), however, this interaction could be weakened greatly by acidification, higher salt concentration (400 mM NaCl) and divalent cation (50 mM Ca2+), which suggests that electrostatic attraction might play an important role in this interaction. In addition, it is noted that two highly conserved amino acids (L218 and L219) in the membrane protein are not involved in this interaction. Here, we show that electrostatic interactions between the carboxyl termini of SARS-CoV membrane protein and nucleocapsid protein largely mediate the interaction of these two proteins. These results might facilitate therapeutic strategies aiming at the disruption of the association between SARS-CoV membrane and nucleocapsid proteins.

DOI: 10.1016/j.biocel.2005.10.022
PubMed: 16343974

Affiliations:

République populaire de Chine

Le document en format XML

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<term>SARS Virus (metabolism)</term>
<term>Static Electricity</term>
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<term>Protéines nucléocapside (métabolisme)</term>
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<front><div type="abstract" xml:lang="en">The severe acute respiratory syndrome coronavirus (SARS-CoV) membrane protein is an abundant virion protein, and its interaction with the nucleocapsid protein is crucial for viral assembly and morphogenesis. Although the interacting region in the nucleocapsid protein was mapped to residues 168-208, the interacting region in the membrane protein and the interaction nature are still unclear. In this work, by using yeast two-hybrid and surface plasmon resonance techniques, the residues 197-221 of the membrane protein and the residues 351-422 of the nucleocapsid protein were determined to be involved in their interaction. Sequence analysis revealed that these two fragments are highly charged at neutral pH, suggesting that their interaction may be of ionic nature. Kinetic assays indicated that the endodomain (aa102-221) of the membrane protein interacts with the nucleocapsid protein with high affinity (K(D)=0.55+/-0.04 microM), however, this interaction could be weakened greatly by acidification, higher salt concentration (400 mM NaCl) and divalent cation (50 mM Ca2+), which suggests that electrostatic attraction might play an important role in this interaction. In addition, it is noted that two highly conserved amino acids (L218 and L219) in the membrane protein are not involved in this interaction. Here, we show that electrostatic interactions between the carboxyl termini of SARS-CoV membrane protein and nucleocapsid protein largely mediate the interaction of these two proteins. These results might facilitate therapeutic strategies aiming at the disruption of the association between SARS-CoV membrane and nucleocapsid proteins.</div>
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Severe acute respiratory syndrome coronavirus membrane protein interacts with nucleocapsid protein mostly through their carboxyl termini by electrostatic attraction.

Severe acute respiratory syndrome coronavirus membrane protein interacts with nucleocapsid protein mostly through their carboxyl termini by electrostatic attraction.

Source :

Descripteurs français

English descriptors

Abstract

Links toward previous steps (curation, corpus...)

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