Structure of the infectious salmon anemia virus receptor complex illustrates a unique binding strategy for attachment
The infectious salmon anemia virus (ISAV), an aquatic pathogen with lethal hemorrhagic potential, decimates farmed and freshwater fish populations globally. Here, we determined the crystallographic structures of the hemagglutinin-esterase (HE) viral glycoprotein responsible for the dynamic attachmen...
| Published in: | Proceedings of the National Academy of Sciences |
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| Main Authors: | , , |
| Format: | Text |
| Language: | English |
| Published: |
National Academy of Sciences
2017
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| Subjects: | |
| Online Access: | http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5389325/ http://www.ncbi.nlm.nih.gov/pubmed/28320973 https://doi.org/10.1073/pnas.1617993114 |
| Summary: | The infectious salmon anemia virus (ISAV), an aquatic pathogen with lethal hemorrhagic potential, decimates farmed and freshwater fish populations globally. Here, we determined the crystallographic structures of the hemagglutinin-esterase (HE) viral glycoprotein responsible for the dynamic attachment of the virus to its receptor in Atlantic salmon. We identified surface features of ISAV HE that are conserved across isolates known to cause significant economic burden to fisheries worldwide. This provides a molecular blueprint for the design of a broadly protective vaccine. Furthermore, we showed that ISAV HE has a distinct receptor recognition strategy from those of other influenza-like viruses and coronaviral HE proteins, contributing to our understanding of the diversity of viral entry mechanisms. |
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