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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Motifs*
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Animals
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Cells, Cultured
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Humans
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Membrane Glycoproteins* / genetics
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Membrane Glycoproteins* / metabolism
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Mice
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Molecular Sequence Data
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Protein Structure, Quaternary*
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Sequence Alignment
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Severe Acute Respiratory Syndrome*
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Severe acute respiratory syndrome-related coronavirus* / genetics
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Severe acute respiratory syndrome-related coronavirus* / metabolism
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Spike Glycoprotein, Coronavirus
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Viral Envelope Proteins* / genetics
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Viral Envelope Proteins* / metabolism
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Virus Internalization*
Substances
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Membrane Glycoproteins
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Spike Glycoprotein, Coronavirus
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Viral Envelope Proteins
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spike glycoprotein, SARS-CoV
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spike protein, mouse hepatitis virus