SrasV1, Main, Exploration, bibRecord, 003B69

GxxxG motif of severe acute respiratory syndrome coronavirus spike glycoprotein transmembrane domain is not involved in trimerization and is not important for entry

Identifieur interne : 003B69 ( Main/Exploration ); précédent : 003B68; suivant : 003B70

GxxxG motif of severe acute respiratory syndrome coronavirus spike glycoprotein transmembrane domain is not involved in trimerization and is not important for entry

Auteurs : Jeroen Corver [Pays-Bas] ; Rene Broer [Pays-Bas] ; Puck Van Kasteren [Pays-Bas] ; Willy Spaan [Pays-Bas]

Source :

Journal of virology [ 0022-538X ] ; 2007.

RBID : Pascal:07-0486287

Descripteurs français

English descriptors

KwdEn :
- Acute, Amino Acid Motifs, Animals, Cells, Cultured, Coronavirus, Glycoprotein, Humans, Membrane Glycoproteins (genetics), Membrane Glycoproteins (metabolism), Mice, Molecular Sequence Data, Protein Structure, Quaternary, SARS Virus (genetics), SARS Virus (metabolism), Sequence Alignment, Severe Acute Respiratory Syndrome, Spike Glycoprotein, Coronavirus, Viral Envelope Proteins (genetics), Viral Envelope Proteins (metabolism), Virology, Virus Internalization.
MESH :
- chemical , genetics : Membrane Glycoproteins, Viral Envelope Proteins.
- chemical , metabolism : Membrane Glycoproteins, Viral Envelope Proteins.
- genetics : SARS Virus.
- metabolism : SARS Virus.
- Amino Acid Motifs, Animals, Cells, Cultured, Humans, Mice, Molecular Sequence Data, Protein Structure, Quaternary, Sequence Alignment, Severe Acute Respiratory Syndrome, Spike Glycoprotein, Coronavirus, Virus Internalization.

Abstract

Recently, a paper was published in which it was proposed that the GxxxG motif of the severe acute respiratory syndrome (SARS) coronavirus spike (S) protein transmembrane domain plays a vital role in oligomerization of the protein (E. Arbely, Z. Granot, I. Kass, J. Orly, and I. T. Arkin, Biochemistry 45:11349-11356, 2006). Here, we show that the GxxxG motif is not involved in SARS S oligomerization by trimerization analysis of S GxxxG mutant proteins. In addition, the capability of S to mediate entry of SARS S-pseudotyped particles overall was affected moderately in the mutant proteins, also arguing for a nonvital role for the GxxxG motif in SARS coronavirus entry.

Affiliations:

Pays-Bas

Le document en format XML

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<term>Cells, Cultured</term>
<term>Humans</term>
<term>Mice</term>
<term>Molecular Sequence Data</term>
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<front><div type="abstract" xml:lang="en">Recently, a paper was published in which it was proposed that the GxxxG motif of the severe acute respiratory syndrome (SARS) coronavirus spike (S) protein transmembrane domain plays a vital role in oligomerization of the protein (E. Arbely, Z. Granot, I. Kass, J. Orly, and I. T. Arkin, Biochemistry 45:11349-11356, 2006). Here, we show that the GxxxG motif is not involved in SARS S oligomerization by trimerization analysis of S GxxxG mutant proteins. In addition, the capability of S to mediate entry of SARS S-pseudotyped particles overall was affected moderately in the mutant proteins, also arguing for a nonvital role for the GxxxG motif in SARS coronavirus entry.</div>
</front>
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<affiliations><list><country><li>Pays-Bas</li>
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<tree><country name="Pays-Bas"><noRegion><name sortKey="Corver, Jeroen" sort="Corver, Jeroen" uniqKey="Corver J" first="Jeroen" last="Corver">Jeroen Corver</name>
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GxxxG motif of severe acute respiratory syndrome coronavirus spike glycoprotein transmembrane domain is not involved in trimerization and is not important for entry

GxxxG motif of severe acute respiratory syndrome coronavirus spike glycoprotein transmembrane domain is not involved in trimerization and is not important for entry

Source :

Descripteurs français

English descriptors

Abstract

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