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Endocytosis of the receptor-binding domain of SARS-CoV spike protein together with virus receptor ACE2.

Identifieur interne : 001B22 ( PubMed/Curation ); précédent : 001B21; suivant : 001B23

Endocytosis of the receptor-binding domain of SARS-CoV spike protein together with virus receptor ACE2.

Auteurs : Shunxin Wang [République populaire de Chine] ; Feng Guo ; Kangtai Liu ; Hongliang Wang ; Shuan Rao ; Peng Yang ; Chengyu Jiang

Source :

Virus research [ 0168-1702 ] ; 2008.

RBID : pubmed:18554741

Descripteurs français

English descriptors

KwdEn :
- Animals, Cell Line, Chlorocebus aethiops, Endocytosis, Flow Cytometry, Humans, Immunoglobulin Fc Fragments (genetics), Membrane Glycoproteins (genetics), Membrane Glycoproteins (metabolism), Peptidyl-Dipeptidase A (metabolism), Protein Binding, Receptors, Virus (metabolism), Recombinant Fusion Proteins (genetics), Recombinant Fusion Proteins (metabolism), SARS Virus (physiology), Spike Glycoprotein, Coronavirus, Viral Envelope Proteins (genetics), Viral Envelope Proteins (metabolism).
MESH :
- chemical , genetics : Immunoglobulin Fc Fragments, Membrane Glycoproteins, Recombinant Fusion Proteins, Viral Envelope Proteins.
- chemical , metabolism : Membrane Glycoproteins, Peptidyl-Dipeptidase A, Receptors, Virus, Recombinant Fusion Proteins, Viral Envelope Proteins.
- physiology : SARS Virus.
- Animals, Cell Line, Chlorocebus aethiops, Endocytosis, Flow Cytometry, Humans, Protein Binding, Spike Glycoprotein, Coronavirus.

Abstract

Cell entry of severe acute respiratory syndrome coronavirus (SARS-CoV) is mediated by the viral spike (S) protein. Amino acids 319-510 on the S protein have been mapped as the receptor-binding domain (RBD), which mediates binding to the SARS-CoV receptor angiotensin converting enzyme 2 (ACE2) on SARS-CoV susceptible cells. In this study, we expressed a fusion protein containing the human codon-optimized RBD of the SARS-CoV spike protein linked to the Fc portion of human IgG1 (named RBD-Fc) in HEK293 cells. The RBD-Fc protein was purified by affinity chromatography. The flow cytometry assay showed that the purified RBD-Fc protein could bind to ACE2. We demonstrated that the RBD spike protein alone could be internalized into SARS-CoV susceptible cells together with ACE2. We also showed that the removal of N-glycans from the RBD spike protein did not abolish this phenomenon. Our discoveries may have some implications for the development of the SARS vaccine.

DOI: 10.1016/j.virusres.2008.03.004
PubMed: 18554741

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Le document en format XML

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<front><div type="abstract" xml:lang="en">Cell entry of severe acute respiratory syndrome coronavirus (SARS-CoV) is mediated by the viral spike (S) protein. Amino acids 319-510 on the S protein have been mapped as the receptor-binding domain (RBD), which mediates binding to the SARS-CoV receptor angiotensin converting enzyme 2 (ACE2) on SARS-CoV susceptible cells. In this study, we expressed a fusion protein containing the human codon-optimized RBD of the SARS-CoV spike protein linked to the Fc portion of human IgG1 (named RBD-Fc) in HEK293 cells. The RBD-Fc protein was purified by affinity chromatography. The flow cytometry assay showed that the purified RBD-Fc protein could bind to ACE2. We demonstrated that the RBD spike protein alone could be internalized into SARS-CoV susceptible cells together with ACE2. We also showed that the removal of N-glycans from the RBD spike protein did not abolish this phenomenon. Our discoveries may have some implications for the development of the SARS vaccine.</div>
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Endocytosis of the receptor-binding domain of SARS-CoV spike protein together with virus receptor ACE2.

Endocytosis of the receptor-binding domain of SARS-CoV spike protein together with virus receptor ACE2.

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