Back to Search
Start Over
Structure and function of respiratory syncytial virus surface glycoproteins.
- Source :
-
Current topics in microbiology and immunology [Curr Top Microbiol Immunol] 2013; Vol. 372, pp. 83-104. - Publication Year :
- 2013
-
Abstract
- The two major glycoproteins on the surface of the respiratory syncytial virus (RSV) virion, the attachment glycoprotein (G) and the fusion glycoprotein (F), control the initial phases of infection. G targets the ciliated cells of the airways, and F causes the virion membrane to fuse with the target cell membrane. The F protein is the major target for antiviral drug development, and both G and F glycoproteins are the antigens targeted by neutralizing antibodies induced by infection. In this chapter, we review the structure and function of the RSV surface glycoproteins, including recent X-ray crystallographic data of the F glycoprotein in its pre- and postfusion conformations, and discuss how this information informs antigen selection and vaccine development.
- Subjects :
- Antibodies, Neutralizing immunology
Antiviral Agents chemical synthesis
Antiviral Agents pharmacology
Cilia immunology
Cilia virology
Humans
Models, Molecular
Protein Conformation
Receptors, Virus chemistry
Receptors, Virus physiology
Respiratory Mucosa immunology
Respiratory Mucosa virology
Respiratory Syncytial Virus Infections immunology
Respiratory Syncytial Virus Vaccines administration & dosage
Respiratory Syncytial Virus, Human drug effects
Respiratory Syncytial Virus, Human immunology
Viral Fusion Proteins antagonists & inhibitors
Viral Fusion Proteins physiology
Virion chemistry
Virion physiology
Antibodies, Viral immunology
Respiratory Syncytial Virus Infections prevention & control
Respiratory Syncytial Virus Vaccines immunology
Respiratory Syncytial Virus, Human chemistry
Viral Fusion Proteins chemistry
Subjects
Details
- Language :
- English
- ISSN :
- 0070-217X
- Volume :
- 372
- Database :
- MEDLINE
- Journal :
- Current topics in microbiology and immunology
- Publication Type :
- Academic Journal
- Accession number :
- 24362685
- Full Text :
- https://doi.org/10.1007/978-3-642-38919-1_4