A single amino acid substitution in the V protein of Nipah virus alters its ability to block interferon signalling in cells from different species
| Autor: | Kathrin Hagmaier, Nicola Stock, Steve Goodbourn, Richard E. Randall, Lin-Fa Wang |
|---|---|
| Rok vydání: | 2006 |
| Předmět: |
Mutant
Plasma protein binding medicine.disease_cause Virus Viral Proteins 03 medical and health sciences Genes Reporter Interferon Virology medicine STAT1 STAT2 Luciferases Gene 030304 developmental biology 0303 health sciences Mutation biology Animal 030306 microbiology Nipah Virus STAT2 Transcription Factor Molecular biology 3. Good health STAT1 Transcription Factor Amino Acid Substitution biology.protein Interferons Protein Binding medicine.drug |
| Zdroj: | The Journal of General Virology |
| ISSN: | 1465-2099 0022-1317 |
| DOI: | 10.1099/vir.0.82261-0 |
| Popis: | The V protein of the paramyxovirus Nipah virus (NiV) has been shown to antagonize the interferon (IFN) response in human cells via sequestration of STAT1 and STAT2. This study describes a mutant of the NiV V protein, referred to as V(AAHL), that is unable to antagonize IFN signalling and demonstrates that a single amino acid substitution is responsible for its inactivity. The molecular basis for this was identified as a failure to interact with STAT1 and STAT2. It was also shown that NiV V, but not V(AAHL), was functional as an IFN antagonist in human, monkey, rabbit, dog, horse, pig and bat cells, which suggests that the ability of NiV to block IFN signalling is not a major constraint that prevents this virus from crossing species barriers. |
| Databáze: | OpenAIRE |
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