Influence of Different Glycoproteins and of the Virion Core on SERINC5 Antiviral Activity
Host plasma membrane protein SERINC5 is incorporated into budding retrovirus particles where it blocks subsequent entry into susceptible target cells. Three structurally unrelated proteins encoded by diverse retroviruses, human immunodeficiency virus type 1 (HIV-1) Nef, equine infectious anemia viru...
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| Format: | Article |
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MDPI AG
2021-06-01
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| Series: | Viruses |
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| Online Access: | https://www.mdpi.com/1999-4915/13/7/1279 |
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| author | William E. Diehl Mehmet H. Guney Teresa Vanzo Pyae P. Kyawe Judith M. White Massimo Pizzato Jeremy Luban |
| author_facet | William E. Diehl Mehmet H. Guney Teresa Vanzo Pyae P. Kyawe Judith M. White Massimo Pizzato Jeremy Luban |
| author_sort | William E. Diehl |
| collection | DOAJ |
| description | Host plasma membrane protein SERINC5 is incorporated into budding retrovirus particles where it blocks subsequent entry into susceptible target cells. Three structurally unrelated proteins encoded by diverse retroviruses, human immunodeficiency virus type 1 (HIV-1) Nef, equine infectious anemia virus (EIAV) S2, and ecotropic murine leukemia virus (MLV) GlycoGag, disrupt SERINC5 antiviral activity by redirecting SERINC5 from the site of virion assembly on the plasma membrane to an internal RAB7+ endosomal compartment. Pseudotyping retroviruses with particular glycoproteins, e.g., vesicular stomatitis virus glycoprotein (VSV G), renders the infectivity of particles resistant to inhibition by virion-associated SERINC5. To better understand viral determinants for SERINC5-sensitivity, the effect of SERINC5 was assessed using HIV-1, MLV, and Mason-Pfizer monkey virus (M-PMV) virion cores, pseudotyped with glycoproteins from Arenavirus, Coronavirus, Filovirus, Rhabdovirus, Paramyxovirus, and Orthomyxovirus genera. SERINC5 restricted virions pseudotyped with glycoproteins from several retroviruses, an orthomyxovirus, a rhabdovirus, a paramyxovirus, and an arenavirus. Infectivity of particles pseudotyped with HIV-1, amphotropic-MLV (A-MLV), or influenza A virus (IAV) glycoproteins, was decreased by SERINC5, whether the core was provided by HIV-1, MLV, or M-PMV. In contrast, particles pseudotyped with glycoproteins from M-PMV, parainfluenza virus 5 (PIV5), or rabies virus (RABV) were sensitive to SERINC5, but only with particular retroviral cores. Resistance to SERINC5 did not correlate with reduced SERINC5 incorporation into particles, route of viral entry, or absolute infectivity of the pseudotyped virions. These findings indicate that some non-retroviruses may be sensitive to SERINC5 and that, in addition to the viral glycoprotein, the retroviral core influences sensitivity to SERINC5. |
| first_indexed | 2024-03-10T09:55:39Z |
| format | Article |
| id | doaj.art-52c34191bdc2468daadae2dbe2a528d4 |
| institution | Directory Open Access Journal |
| issn | 1999-4915 |
| language | English |
| last_indexed | 2024-03-10T09:55:39Z |
| publishDate | 2021-06-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Viruses |
| spelling | doaj.art-52c34191bdc2468daadae2dbe2a528d42023-11-22T02:23:22ZengMDPI AGViruses1999-49152021-06-01137127910.3390/v13071279Influence of Different Glycoproteins and of the Virion Core on SERINC5 Antiviral ActivityWilliam E. Diehl0Mehmet H. Guney1Teresa Vanzo2Pyae P. Kyawe3Judith M. White4Massimo Pizzato5Jeremy Luban6Program in Molecular Medicine, University of Massachusetts Medical School, 373 Plantation Street, Worcester, MA 01605, USAProgram in Molecular Medicine, University of Massachusetts Medical School, 373 Plantation Street, Worcester, MA 01605, USADepartment of Cellular, Computational and Integrative Biology, University of Trento, 38123 Trento, ItalyProgram in Molecular Medicine, University of Massachusetts Medical School, 373 Plantation Street, Worcester, MA 01605, USADepartment of Cell Biology, University of Virginia, Charlottesville, VA 22908, USADepartment of Cellular, Computational and Integrative Biology, University of Trento, 38123 Trento, ItalyProgram in Molecular Medicine, University of Massachusetts Medical School, 373 Plantation Street, Worcester, MA 01605, USAHost plasma membrane protein SERINC5 is incorporated into budding retrovirus particles where it blocks subsequent entry into susceptible target cells. Three structurally unrelated proteins encoded by diverse retroviruses, human immunodeficiency virus type 1 (HIV-1) Nef, equine infectious anemia virus (EIAV) S2, and ecotropic murine leukemia virus (MLV) GlycoGag, disrupt SERINC5 antiviral activity by redirecting SERINC5 from the site of virion assembly on the plasma membrane to an internal RAB7+ endosomal compartment. Pseudotyping retroviruses with particular glycoproteins, e.g., vesicular stomatitis virus glycoprotein (VSV G), renders the infectivity of particles resistant to inhibition by virion-associated SERINC5. To better understand viral determinants for SERINC5-sensitivity, the effect of SERINC5 was assessed using HIV-1, MLV, and Mason-Pfizer monkey virus (M-PMV) virion cores, pseudotyped with glycoproteins from Arenavirus, Coronavirus, Filovirus, Rhabdovirus, Paramyxovirus, and Orthomyxovirus genera. SERINC5 restricted virions pseudotyped with glycoproteins from several retroviruses, an orthomyxovirus, a rhabdovirus, a paramyxovirus, and an arenavirus. Infectivity of particles pseudotyped with HIV-1, amphotropic-MLV (A-MLV), or influenza A virus (IAV) glycoproteins, was decreased by SERINC5, whether the core was provided by HIV-1, MLV, or M-PMV. In contrast, particles pseudotyped with glycoproteins from M-PMV, parainfluenza virus 5 (PIV5), or rabies virus (RABV) were sensitive to SERINC5, but only with particular retroviral cores. Resistance to SERINC5 did not correlate with reduced SERINC5 incorporation into particles, route of viral entry, or absolute infectivity of the pseudotyped virions. These findings indicate that some non-retroviruses may be sensitive to SERINC5 and that, in addition to the viral glycoprotein, the retroviral core influences sensitivity to SERINC5.https://www.mdpi.com/1999-4915/13/7/1279retrovirusesglycoproteinsrestriction factorSERINC5gagvirion |
| spellingShingle | William E. Diehl Mehmet H. Guney Teresa Vanzo Pyae P. Kyawe Judith M. White Massimo Pizzato Jeremy Luban Influence of Different Glycoproteins and of the Virion Core on SERINC5 Antiviral Activity Viruses retroviruses glycoproteins restriction factor SERINC5 gag virion |
| title | Influence of Different Glycoproteins and of the Virion Core on SERINC5 Antiviral Activity |
| title_full | Influence of Different Glycoproteins and of the Virion Core on SERINC5 Antiviral Activity |
| title_fullStr | Influence of Different Glycoproteins and of the Virion Core on SERINC5 Antiviral Activity |
| title_full_unstemmed | Influence of Different Glycoproteins and of the Virion Core on SERINC5 Antiviral Activity |
| title_short | Influence of Different Glycoproteins and of the Virion Core on SERINC5 Antiviral Activity |
| title_sort | influence of different glycoproteins and of the virion core on serinc5 antiviral activity |
| topic | retroviruses glycoproteins restriction factor SERINC5 gag virion |
| url | https://www.mdpi.com/1999-4915/13/7/1279 |
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