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Expression, glycosylation, and modification of the spike (S) glycoprotein of SARS CoV.

Identifieur interne : 003706 ( Main/Exploration ); précédent : 003705; suivant : 003707

Expression, glycosylation, and modification of the spike (S) glycoprotein of SARS CoV.

Auteurs : Shuo Shen [Singapour] ; Timothy H P. Tan ; Yee-Joo Tan

Source :

RBID : pubmed:17502675

Descripteurs français

English descriptors

Abstract

The spike (S) glycoprotein of coronaviruses is known to be essential in the binding of the virus to the host cell at the advent of the infection process. To study the maturation pathway of the S glycoprotein of the severe acute respiratory syndrome (SARS)-coronavirus (CoV) within the host cell, a T7/vaccinia virus-based expression system coupled to immunoprecipitation with anti-S antibodies was used to test and analyze different forms of the S glycoprotein. The state of maturity of the S glycoprotein can be deduced from its sensitivity to hydrolysis by endoglycosidase H (EndoH) or N-glycosidase F (N-Gly F). A fully matured S glycoprotein will be modified with complex oligosaccharides which makes it resistant to cleavage by EndoH but not by N-Gly F. By exploiting this characteristic, it is then possible to determine which forms of the immunoprecipitated S protein are properly processed by the host cell. With this system, many different constructs of the S glycoprotein can be analyzed in parallel thus providing another method by which to study the functional domains of S involved in membrane fusion event that occurs during viral infection.

DOI: 10.1007/978-1-59745-393-6_9
PubMed: 17502675


Affiliations:

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Le document en format XML

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<term>Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase (chemistry)</term>
<term>Membrane Glycoproteins (analysis)</term>
<term>Membrane Glycoproteins (biosynthesis)</term>
<term>Membrane Glycoproteins (genetics)</term>
<term>Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase (chemistry)</term>
<term>Protein Modification, Translational (physiology)</term>
<term>Recombinant Proteins (analysis)</term>
<term>Recombinant Proteins (biosynthesis)</term>
<term>Recombinant Proteins (genetics)</term>
<term>SARS Virus (genetics)</term>
<term>Spike Glycoprotein, Coronavirus</term>
<term>Vaccinia virus (genetics)</term>
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<term>Viral Envelope Proteins (biosynthesis)</term>
<term>Viral Envelope Proteins (genetics)</term>
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<term>Animaux</term>
<term>Cellules COS</term>
<term>Cellules Vero</term>
<term>Expression des gènes</term>
<term>Glycoprotéine de spicule des coronavirus</term>
<term>Glycoprotéines membranaires (analyse)</term>
<term>Glycoprotéines membranaires (biosynthèse)</term>
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<term>Protéines de l'enveloppe virale (analyse)</term>
<term>Protéines de l'enveloppe virale (biosynthèse)</term>
<term>Protéines de l'enveloppe virale (génétique)</term>
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<div type="abstract" xml:lang="en">The spike (S) glycoprotein of coronaviruses is known to be essential in the binding of the virus to the host cell at the advent of the infection process. To study the maturation pathway of the S glycoprotein of the severe acute respiratory syndrome (SARS)-coronavirus (CoV) within the host cell, a T7/vaccinia virus-based expression system coupled to immunoprecipitation with anti-S antibodies was used to test and analyze different forms of the S glycoprotein. The state of maturity of the S glycoprotein can be deduced from its sensitivity to hydrolysis by endoglycosidase H (EndoH) or N-glycosidase F (N-Gly F). A fully matured S glycoprotein will be modified with complex oligosaccharides which makes it resistant to cleavage by EndoH but not by N-Gly F. By exploiting this characteristic, it is then possible to determine which forms of the immunoprecipitated S protein are properly processed by the host cell. With this system, many different constructs of the S glycoprotein can be analyzed in parallel thus providing another method by which to study the functional domains of S involved in membrane fusion event that occurs during viral infection.</div>
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