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Event: 2193
Key Event Title
Influenza A Virus (IAV) budding
Short name
Biological Context
Level of Biological Organization |
---|
Cellular |
Cell term
Cell term |
---|
epithelial cell |
Organ term
Organ term |
---|
respiratory tract |
Key Event Components
Process | Object | Action |
---|---|---|
viral budding from plasma membrane | occurrence |
Key Event Overview
AOPs Including This Key Event
AOP Name | Role of event in AOP | Point of Contact | Author Status | OECD Status |
---|---|---|---|---|
IAV infection proliferation | KeyEvent | Jessica Resnick (send email) | Under development: Not open for comment. Do not cite |
Taxonomic Applicability
Life Stages
Sex Applicability
Key Event Description
IAV buds from lipid “rafts” present on the apical membrane (2). Once all the viral components have localized to the site of budding, curvature of the membrane is induced using a combination of molecular crowding and bending proteins. NA and HA proteins are sufficient to induce budding, and the M1 protein contributes to shape and size uniformity of the resulting virions (1,3,4,5,6,7). The M2 protein has also been shown to contribute to membrane bending and scission (8). After budding, release is mediated by the sialidase property of NA. The NA protein catalyzes the hydrolysis of all sialic acid attachments made by the HA protein allowing for the virus to be released from the cell membrane (1,9,10).
How It Is Measured or Detected
Technique |
Conclusions/ uses |
Example Reference |
Virus- like particles |
Measure specific contributions of proteins to the viral life cycle |
|
Electron microscopy |
Visualize budding |
Chlanda P, Schraidt O, Kummer S, Riches J, Oberwinkler H, Prinz S, et al. Structural analysis of the roles of influenza A virus membrane-associated proteins in assembly and morphology. J Virol (2015) 89:8957–66. 10.1128/JVI.00592-15 |
Domain of Applicability
References
- Dou, D., Revol, R., Ostbye, H., Wang, H., and Daniels, R., Influenza A Virus Cell Entry, Replication, Virion Assembly and Movement. Front. Immunol. 20 July 2018. https://doi.org/10.3389/fimmu.2018.01581
- Lingwood D, Simons K. Lipid rafts as a membrane-organizing principle. Science (2010) 327:46–50. 10.1126/science.1174621
- Chen BJ, Leser GP, Morita E, Lamb RA. Influenza virus hemagglutinin and neuraminidase, but not the matrix protein, are required for assembly and budding of plasmid-derived virus-like particles. J Virol (2007) 81:7111–23. 10.1128/JVI.00361-07
- Lai JC, Chan WW, Kien F, Nicholls JM, Peiris JS, Garcia JM. Formation of virus-like particles from human cell lines exclusively expressing influenza neuraminidase. J Gen Virol (2010) 91:2322–30. 10.1099/vir.0.019935-0
- Yondola MA, Fernandes F, Belicha-Villanueva A, Uccelini M, Gao Q, Carter C, et al. Budding capability of the influenza virus neuraminidase can be modulated by tetherin. J Virol (2011) 85:2480–91. 10.1128/JVI.02188-10
- Chlanda P, Schraidt O, Kummer S, Riches J, Oberwinkler H, Prinz S, et al. Structural analysis of the roles of influenza A virus membrane-associated proteins in assembly and morphology. J Virol (2015) 89:8957–66. 10.1128/JVI.00592-15
- Elleman CJ, Barclay WS. The M1 matrix protein controls the filamentous phenotype of influenza A virus. Virology (2004) 321:144–53. 10.1016/j.virol.2003.12.009
- Rossman JS, Lamb RA. Viral membrane scission. Annu Rev Cell Dev Biol (2013) 29:551–69. 10.1146/annurev-cellbio-101011-155838
- Webster RG, Laver WG. Preparation and properties of antibody directed specifically against the neuraminidase of influenza virus. J Immunol(1967) 99:49–55.
- Palese P, Compans RW. Inhibition of influenza virus replication in tissue culture by 2-deoxy-2,3-dehydro-N-trifluoroacetylneuraminic acid (FANA): mechanism of action. J Gen Virol (1976) 33:159–63. 10.1099/0022-1317-33-1-159