GxxxG Motif of Severe Acute Respiratory Syndrome Coronavirus Spike Glycoprotein Transmembrane Domain Is Not Involved in Trimerization and Is Not Important for Entry
| Autor: | Puck B. van Kasteren, Willy J. M. Spaan, Jeroen Corver, Rene Broer |
|---|---|
| Rok vydání: | 2007 |
| Předmět: |
Amino Acid Motifs
Molecular Sequence Data Immunology Mutant Sequence alignment Severe Acute Respiratory Syndrome medicine.disease_cause Microbiology Mice Protein structure Viral Envelope Proteins Nidovirales Virology medicine Animals Humans Coronaviridae Protein Structure Quaternary skin and connective tissue diseases Cells Cultured Coronavirus chemistry.chemical_classification Membrane Glycoproteins biology fungi Virus Internalization biology.organism_classification Virus-Cell Interactions body regions Transmembrane domain Severe acute respiratory syndrome-related coronavirus chemistry Insect Science Spike Glycoprotein Coronavirus Glycoprotein Sequence Alignment |
| Zdroj: | Journal of Virology |
| ISSN: | 1098-5514 0022-538X |
| DOI: | 10.1128/jvi.00014-07 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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