The Effects of Viral Structural Proteins on Acidic Phospholipids in Host Membranes
Enveloped viruses rely on host membranes for trafficking and assembly. A substantial body of literature published over the years supports the involvement of cellular membrane lipids in the enveloped virus assembly processes. In particular, the knowledge regarding the relationship between viral struc...
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2024-10-01
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| Series: | Viruses |
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| Online Access: | https://www.mdpi.com/1999-4915/16/11/1714 |
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| author | Ricardo de Souza Cardoso Akira Ono |
| author_facet | Ricardo de Souza Cardoso Akira Ono |
| author_sort | Ricardo de Souza Cardoso |
| collection | DOAJ |
| description | Enveloped viruses rely on host membranes for trafficking and assembly. A substantial body of literature published over the years supports the involvement of cellular membrane lipids in the enveloped virus assembly processes. In particular, the knowledge regarding the relationship between viral structural proteins and acidic phospholipids has been steadily increasing in recent years. In this review, we will briefly review the cellular functions of plasma membrane-associated acidic phospholipids and the mechanisms that regulate their local distribution within this membrane. We will then explore the interplay between viruses and the plasma membrane acidic phospholipids in the context of the assembly process for two enveloped viruses, the influenza A virus (IAV) and the human immunodeficiency virus type 1 (HIV-1). Among the proteins encoded by these viruses, three viral structural proteins, IAV hemagglutinin (HA), IAV matrix protein-1 (M1), and HIV-1 Gag protein, are known to interact with acidic phospholipids, phosphatidylserine and/or phosphatidylinositol (4,5)-bisphosphate. These interactions regulate the localization of the viral proteins to and/or within the plasma membrane and likely facilitate the clustering of the proteins. On the other hand, these viral proteins, via their ability to multimerize, can also alter the distribution of the lipids and may induce acidic-lipid-enriched membrane domains. We will discuss the potential significance of these interactions in the virus assembly process and the property of the progeny virions. Finally, we will outline key outstanding questions that need to be answered for a better understanding of the relationships between enveloped virus assembly and acidic phospholipids. |
| format | Article |
| id | doaj-art-d2053bcff6a24a4489d145903d65cc63 |
| institution | Kabale University |
| issn | 1999-4915 |
| language | English |
| publishDate | 2024-10-01 |
| publisher | MDPI AG |
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| series | Viruses |
| spelling | doaj-art-d2053bcff6a24a4489d145903d65cc632024-11-26T18:25:24ZengMDPI AGViruses1999-49152024-10-011611171410.3390/v16111714The Effects of Viral Structural Proteins on Acidic Phospholipids in Host MembranesRicardo de Souza Cardoso0Akira Ono1Department of Microbiology and Immunology, The University of Michigan, Ann Arbor, MI 48109, USADepartment of Microbiology and Immunology, The University of Michigan, Ann Arbor, MI 48109, USAEnveloped viruses rely on host membranes for trafficking and assembly. A substantial body of literature published over the years supports the involvement of cellular membrane lipids in the enveloped virus assembly processes. In particular, the knowledge regarding the relationship between viral structural proteins and acidic phospholipids has been steadily increasing in recent years. In this review, we will briefly review the cellular functions of plasma membrane-associated acidic phospholipids and the mechanisms that regulate their local distribution within this membrane. We will then explore the interplay between viruses and the plasma membrane acidic phospholipids in the context of the assembly process for two enveloped viruses, the influenza A virus (IAV) and the human immunodeficiency virus type 1 (HIV-1). Among the proteins encoded by these viruses, three viral structural proteins, IAV hemagglutinin (HA), IAV matrix protein-1 (M1), and HIV-1 Gag protein, are known to interact with acidic phospholipids, phosphatidylserine and/or phosphatidylinositol (4,5)-bisphosphate. These interactions regulate the localization of the viral proteins to and/or within the plasma membrane and likely facilitate the clustering of the proteins. On the other hand, these viral proteins, via their ability to multimerize, can also alter the distribution of the lipids and may induce acidic-lipid-enriched membrane domains. We will discuss the potential significance of these interactions in the virus assembly process and the property of the progeny virions. Finally, we will outline key outstanding questions that need to be answered for a better understanding of the relationships between enveloped virus assembly and acidic phospholipids.https://www.mdpi.com/1999-4915/16/11/1714influenza A virus (IAV)human immunodeficiency virus (HIV-1)acidic phospholipidsphosphatidylinositol (4.5)-bisphosphate (PI(4,5)P2)phosphatidylserine (PS)virus assembly |
| spellingShingle | Ricardo de Souza Cardoso Akira Ono The Effects of Viral Structural Proteins on Acidic Phospholipids in Host Membranes Viruses influenza A virus (IAV) human immunodeficiency virus (HIV-1) acidic phospholipids phosphatidylinositol (4.5)-bisphosphate (PI(4,5)P2) phosphatidylserine (PS) virus assembly |
| title | The Effects of Viral Structural Proteins on Acidic Phospholipids in Host Membranes |
| title_full | The Effects of Viral Structural Proteins on Acidic Phospholipids in Host Membranes |
| title_fullStr | The Effects of Viral Structural Proteins on Acidic Phospholipids in Host Membranes |
| title_full_unstemmed | The Effects of Viral Structural Proteins on Acidic Phospholipids in Host Membranes |
| title_short | The Effects of Viral Structural Proteins on Acidic Phospholipids in Host Membranes |
| title_sort | effects of viral structural proteins on acidic phospholipids in host membranes |
| topic | influenza A virus (IAV) human immunodeficiency virus (HIV-1) acidic phospholipids phosphatidylinositol (4.5)-bisphosphate (PI(4,5)P2) phosphatidylserine (PS) virus assembly |
| url | https://www.mdpi.com/1999-4915/16/11/1714 |
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