Hantavirus Gn and Gc Envelope Glycoproteins: Key Structural Units for Virus Cell Entry and Virus Assembly
In recent years, ultrastructural studies of viral surface spikes from three different genera within the Bunyaviridae family have revealed a remarkable diversity in their spike organization. Despite this structural heterogeneity, in every case the spikes seem to be composed of heterodimers formed by...
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| Format: | Article |
| Language: | English |
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MDPI AG
2014-04-01
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| Series: | Viruses |
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| Online Access: | http://www.mdpi.com/1999-4915/6/4/1801 |
| _version_ | 1818837684006682624 |
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| author | Nicolás Cifuentes-Muñoz Natalia Salazar-Quiroz Nicole D. Tischler |
| author_facet | Nicolás Cifuentes-Muñoz Natalia Salazar-Quiroz Nicole D. Tischler |
| author_sort | Nicolás Cifuentes-Muñoz |
| collection | DOAJ |
| description | In recent years, ultrastructural studies of viral surface spikes from three different genera within the Bunyaviridae family have revealed a remarkable diversity in their spike organization. Despite this structural heterogeneity, in every case the spikes seem to be composed of heterodimers formed by Gn and Gc envelope glycoproteins. In this review, current knowledge of the Gn and Gc structures and their functions in virus cell entry and exit is summarized. During virus cell entry, the role of Gn and Gc in receptor binding has not yet been determined. Nevertheless, biochemical studies suggest that the subsequent virus-membrane fusion activity is accomplished by Gc. Further, a class II fusion protein conformation has been predicted for Gc of hantaviruses, and novel crystallographic data confirmed such a fold for the Rift Valley fever virus (RVFV) Gc protein. During virus cell exit, the assembly of different viral components seems to be established by interaction of Gn and Gc cytoplasmic tails (CT) with internal viral ribonucleocapsids. Moreover, recent findings show that hantavirus glycoproteins accomplish important roles during virus budding since they self-assemble into virus-like particles. Collectively, these novel insights provide essential information for gaining a more detailed understanding of Gn and Gc functions in the early and late steps of the hantavirus infection cycle. |
| first_indexed | 2024-12-19T03:26:24Z |
| format | Article |
| id | doaj.art-a6668d0bd15c44c0a45588634e57171f |
| institution | Directory Open Access Journal |
| issn | 1999-4915 |
| language | English |
| last_indexed | 2024-12-19T03:26:24Z |
| publishDate | 2014-04-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Viruses |
| spelling | doaj.art-a6668d0bd15c44c0a45588634e57171f2022-12-21T20:37:36ZengMDPI AGViruses1999-49152014-04-01641801182210.3390/v6041801v6041801Hantavirus Gn and Gc Envelope Glycoproteins: Key Structural Units for Virus Cell Entry and Virus AssemblyNicolás Cifuentes-Muñoz0Natalia Salazar-Quiroz1Nicole D. Tischler2Molecular Virology Laboratory, Fundación Ciencia & Vida, Av. Zañartu 1482, Ñuñoa, Santiago 7780272, ChileMolecular Virology Laboratory, Fundación Ciencia & Vida, Av. Zañartu 1482, Ñuñoa, Santiago 7780272, ChileMolecular Virology Laboratory, Fundación Ciencia & Vida, Av. Zañartu 1482, Ñuñoa, Santiago 7780272, ChileIn recent years, ultrastructural studies of viral surface spikes from three different genera within the Bunyaviridae family have revealed a remarkable diversity in their spike organization. Despite this structural heterogeneity, in every case the spikes seem to be composed of heterodimers formed by Gn and Gc envelope glycoproteins. In this review, current knowledge of the Gn and Gc structures and their functions in virus cell entry and exit is summarized. During virus cell entry, the role of Gn and Gc in receptor binding has not yet been determined. Nevertheless, biochemical studies suggest that the subsequent virus-membrane fusion activity is accomplished by Gc. Further, a class II fusion protein conformation has been predicted for Gc of hantaviruses, and novel crystallographic data confirmed such a fold for the Rift Valley fever virus (RVFV) Gc protein. During virus cell exit, the assembly of different viral components seems to be established by interaction of Gn and Gc cytoplasmic tails (CT) with internal viral ribonucleocapsids. Moreover, recent findings show that hantavirus glycoproteins accomplish important roles during virus budding since they self-assemble into virus-like particles. Collectively, these novel insights provide essential information for gaining a more detailed understanding of Gn and Gc functions in the early and late steps of the hantavirus infection cycle.http://www.mdpi.com/1999-4915/6/4/1801hantavirusenvelopeglycoproteincell entryfusionbiogenesisassemblybuddingstructure |
| spellingShingle | Nicolás Cifuentes-Muñoz Natalia Salazar-Quiroz Nicole D. Tischler Hantavirus Gn and Gc Envelope Glycoproteins: Key Structural Units for Virus Cell Entry and Virus Assembly Viruses hantavirus envelope glycoprotein cell entry fusion biogenesis assembly budding structure |
| title | Hantavirus Gn and Gc Envelope Glycoproteins: Key Structural Units for Virus Cell Entry and Virus Assembly |
| title_full | Hantavirus Gn and Gc Envelope Glycoproteins: Key Structural Units for Virus Cell Entry and Virus Assembly |
| title_fullStr | Hantavirus Gn and Gc Envelope Glycoproteins: Key Structural Units for Virus Cell Entry and Virus Assembly |
| title_full_unstemmed | Hantavirus Gn and Gc Envelope Glycoproteins: Key Structural Units for Virus Cell Entry and Virus Assembly |
| title_short | Hantavirus Gn and Gc Envelope Glycoproteins: Key Structural Units for Virus Cell Entry and Virus Assembly |
| title_sort | hantavirus gn and gc envelope glycoproteins key structural units for virus cell entry and virus assembly |
| topic | hantavirus envelope glycoprotein cell entry fusion biogenesis assembly budding structure |
| url | http://www.mdpi.com/1999-4915/6/4/1801 |
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