Requirements for Human Respiratory Syncytial Virus Glycoproteins in Assembly and Egress from Infected Cells
Human respiratory syncytial virus (HRSV) is an enveloped RNA virus that assembles and buds from the plasma membrane of infected cells. The ribonucleoprotein complex (RNP) must associate with the viral matrix protein and glycoproteins to form newly infectious particles prior to budding. The viral p...
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| Format: | Article |
| Language: | English |
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Wiley
2011-01-01
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| Series: | Advances in Virology |
| Online Access: | http://dx.doi.org/10.1155/2011/343408 |
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| author | Melissa Batonick Gail W. Wertz |
| author_facet | Melissa Batonick Gail W. Wertz |
| author_sort | Melissa Batonick |
| collection | DOAJ |
| description | Human respiratory syncytial virus (HRSV) is an enveloped RNA virus that assembles and buds from the plasma membrane of infected cells. The ribonucleoprotein complex (RNP) must associate with the viral matrix protein and glycoproteins to form newly infectious particles prior to budding. The viral proteins involved in HRSV assembly and egress are mostly unexplored. We investigated whether the glycoproteins of HRSV were involved in the late stages of viral replication by utilizing recombinant viruses where each individual glycoprotein gene was deleted and replaced with a reporter gene to maintain wild-type levels of gene expression. These engineered viruses allowed us to study the roles of the glycoproteins in assembly and budding in the context of infectious virus. Microscopy data showed that the F glycoprotein was involved in the localization of the glycoproteins with the other viral proteins at the plasma membrane. Biochemical analyses showed that deletion of the F and G proteins affected incorporation of the other viral proteins into budded virions. However, efficient viral release was unaffected by the deletion of any of the glycoproteins individually or in concert. These studies attribute a novel role to the F and G proteins in viral protein localization and assembly. |
| format | Article |
| id | doaj-art-9ae77eb94e7c468da80bb0b21c2005ae |
| institution | Kabale University |
| issn | 1687-8639 1687-8647 |
| language | English |
| publishDate | 2011-01-01 |
| publisher | Wiley |
| record_format | Article |
| series | Advances in Virology |
| spelling | doaj-art-9ae77eb94e7c468da80bb0b21c2005ae2025-08-20T03:36:57ZengWileyAdvances in Virology1687-86391687-86472011-01-01201110.1155/2011/343408343408Requirements for Human Respiratory Syncytial Virus Glycoproteins in Assembly and Egress from Infected CellsMelissa Batonick0Gail W. Wertz1Department of Pathology, University of Virginia, MR5 Building, P.O. Box 800904, Charlottesville, VA 22908-0904, USADepartment of Pathology, University of Virginia, MR5 Building, P.O. Box 800904, Charlottesville, VA 22908-0904, USAHuman respiratory syncytial virus (HRSV) is an enveloped RNA virus that assembles and buds from the plasma membrane of infected cells. The ribonucleoprotein complex (RNP) must associate with the viral matrix protein and glycoproteins to form newly infectious particles prior to budding. The viral proteins involved in HRSV assembly and egress are mostly unexplored. We investigated whether the glycoproteins of HRSV were involved in the late stages of viral replication by utilizing recombinant viruses where each individual glycoprotein gene was deleted and replaced with a reporter gene to maintain wild-type levels of gene expression. These engineered viruses allowed us to study the roles of the glycoproteins in assembly and budding in the context of infectious virus. Microscopy data showed that the F glycoprotein was involved in the localization of the glycoproteins with the other viral proteins at the plasma membrane. Biochemical analyses showed that deletion of the F and G proteins affected incorporation of the other viral proteins into budded virions. However, efficient viral release was unaffected by the deletion of any of the glycoproteins individually or in concert. These studies attribute a novel role to the F and G proteins in viral protein localization and assembly.http://dx.doi.org/10.1155/2011/343408 |
| spellingShingle | Melissa Batonick Gail W. Wertz Requirements for Human Respiratory Syncytial Virus Glycoproteins in Assembly and Egress from Infected Cells Advances in Virology |
| title | Requirements for Human Respiratory Syncytial Virus Glycoproteins in Assembly and Egress from Infected Cells |
| title_full | Requirements for Human Respiratory Syncytial Virus Glycoproteins in Assembly and Egress from Infected Cells |
| title_fullStr | Requirements for Human Respiratory Syncytial Virus Glycoproteins in Assembly and Egress from Infected Cells |
| title_full_unstemmed | Requirements for Human Respiratory Syncytial Virus Glycoproteins in Assembly and Egress from Infected Cells |
| title_short | Requirements for Human Respiratory Syncytial Virus Glycoproteins in Assembly and Egress from Infected Cells |
| title_sort | requirements for human respiratory syncytial virus glycoproteins in assembly and egress from infected cells |
| url | http://dx.doi.org/10.1155/2011/343408 |
| work_keys_str_mv | AT melissabatonick requirementsforhumanrespiratorysyncytialvirusglycoproteinsinassemblyandegressfrominfectedcells AT gailwwertz requirementsforhumanrespiratorysyncytialvirusglycoproteinsinassemblyandegressfrominfectedcells |