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VP5* Rearranges when Rotavirus Uncoats
Trypsin primes rotavirus for efficient infectivity by cleaving the spike protein, VP4, into VP8* and VP5*. A recombinant VP5* fragment has a trimeric, folded-back structure. Comparison of this structure with virion spikes suggests that a rearrangement, analogous to those of enveloped virus fusion pr...
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| Hlavní autoři: | , , , , , , , |
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| Médium: | Artigo |
| Jazyk: | Inglês |
| Vydáno: |
American Society for Microbiology (ASM)
2009
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| Témata: | |
| On-line přístup: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2772785/ https://ncbi.nlm.nih.gov/pubmed/19692464 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1128/JVI.01228-09 |
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