Influenza B Virus Receptor Specificity: Closing the Gap between Binding and Tropism
Influenza A and influenza B viruses (FLUAV and FLUBV, respectively) cause significant respiratory disease, hospitalization, and mortality each year. Despite causing at least 25% of the annual disease burden, FLUBV is historically understudied. Unlike FLUAVs, which possess pandemic potential due to t...
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MDPI AG
2024-08-01
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| author | Caroline K. Page Stephen Mark Tompkins |
| author_facet | Caroline K. Page Stephen Mark Tompkins |
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| description | Influenza A and influenza B viruses (FLUAV and FLUBV, respectively) cause significant respiratory disease, hospitalization, and mortality each year. Despite causing at least 25% of the annual disease burden, FLUBV is historically understudied. Unlike FLUAVs, which possess pandemic potential due to their many subtypes and broad host range, FLUBVs are thought to be restricted to only humans and are limited to two lineages. The hemagglutinins (HA) of both influenza types bind glycans terminating in α2,6- or α2,3-sialic acids. For FLUAV, the tropism of human- and avian-origin viruses is well-defined and determined by the terminal sialic acid configuration the HA can accommodate, with avian-origin viruses binding α2,3-linked sialic acids and human-origin viruses binding α2,6-linked sialic acids. In contrast, less is known about FLUBV receptor binding and its impact on host tropism. This review discusses the current literature on FLUBV receptor specificity, HA glycosylation, and their roles in virus tropism, evolution, and infection. While the focus is on findings in the past dozen years, it should be noted that the most current approaches for measuring virus–glycan interactions have not yet been applied to FLUBV and knowledge gaps remain. |
| format | Article |
| id | doaj-art-d1bb5e4eca9f40b38ada81df2fa66cd9 |
| institution | OA Journals |
| issn | 1999-4915 |
| language | English |
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| spelling | doaj-art-d1bb5e4eca9f40b38ada81df2fa66cd92025-08-20T01:56:13ZengMDPI AGViruses1999-49152024-08-01169135610.3390/v16091356Influenza B Virus Receptor Specificity: Closing the Gap between Binding and TropismCaroline K. Page0Stephen Mark Tompkins1Center for Vaccines and Immunology, University of Georgia, Athens, GA 30605, USACenter for Vaccines and Immunology, University of Georgia, Athens, GA 30605, USAInfluenza A and influenza B viruses (FLUAV and FLUBV, respectively) cause significant respiratory disease, hospitalization, and mortality each year. Despite causing at least 25% of the annual disease burden, FLUBV is historically understudied. Unlike FLUAVs, which possess pandemic potential due to their many subtypes and broad host range, FLUBVs are thought to be restricted to only humans and are limited to two lineages. The hemagglutinins (HA) of both influenza types bind glycans terminating in α2,6- or α2,3-sialic acids. For FLUAV, the tropism of human- and avian-origin viruses is well-defined and determined by the terminal sialic acid configuration the HA can accommodate, with avian-origin viruses binding α2,3-linked sialic acids and human-origin viruses binding α2,6-linked sialic acids. In contrast, less is known about FLUBV receptor binding and its impact on host tropism. This review discusses the current literature on FLUBV receptor specificity, HA glycosylation, and their roles in virus tropism, evolution, and infection. While the focus is on findings in the past dozen years, it should be noted that the most current approaches for measuring virus–glycan interactions have not yet been applied to FLUBV and knowledge gaps remain.https://www.mdpi.com/1999-4915/16/9/1356influenza BFLUBVreceptor bindingglycosylationsialic acidsvirus–host interactions |
| spellingShingle | Caroline K. Page Stephen Mark Tompkins Influenza B Virus Receptor Specificity: Closing the Gap between Binding and Tropism Viruses influenza B FLUBV receptor binding glycosylation sialic acids virus–host interactions |
| title | Influenza B Virus Receptor Specificity: Closing the Gap between Binding and Tropism |
| title_full | Influenza B Virus Receptor Specificity: Closing the Gap between Binding and Tropism |
| title_fullStr | Influenza B Virus Receptor Specificity: Closing the Gap between Binding and Tropism |
| title_full_unstemmed | Influenza B Virus Receptor Specificity: Closing the Gap between Binding and Tropism |
| title_short | Influenza B Virus Receptor Specificity: Closing the Gap between Binding and Tropism |
| title_sort | influenza b virus receptor specificity closing the gap between binding and tropism |
| topic | influenza B FLUBV receptor binding glycosylation sialic acids virus–host interactions |
| url | https://www.mdpi.com/1999-4915/16/9/1356 |
| work_keys_str_mv | AT carolinekpage influenzabvirusreceptorspecificityclosingthegapbetweenbindingandtropism AT stephenmarktompkins influenzabvirusreceptorspecificityclosingthegapbetweenbindingandtropism |