Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
Review
. 2015 Apr:11:70-5.
doi: 10.1016/j.coviro.2015.03.002. Epub 2015 Mar 26.

Neutralizing epitopes on the respiratory syncytial virus fusion glycoprotein

Jason S McLellan  1
Affiliations
Review

Neutralizing epitopes on the respiratory syncytial virus fusion glycoprotein

Jason S McLellan. Curr Opin Virol. 2015 Apr.

Abstract

Respiratory syncytial virus (RSV) is a leading cause of pneumonia and bronchiolitis, but despite decades of research a safe and effective vaccine has remained elusive. The viral fusion glycoprotein (RSV F) plays an obligatory role in the entry process and is the major target of neutralizing antibodies, making it an attractive target for vaccine development. This review will summarize the recently determined structures of RSV F in the prefusion and postfusion conformations and describe the location and properties of neutralizing epitopes on RSV F, including the newly identified prefusion-specific epitopes. The influence of these findings on vaccine development will also be discussed, with a focus on the rational design and optimization of vaccine antigens.

PubMed Disclaimer

Figures

Figure 1
Figure 1
Conformations of the RSV F ectodomain. (a) Structures of trimeric RSV F in the prefusion (left) and postfusion (right) conformations. A molecular surface is shown for two of the protomers, colored gray and white, whereas the third protomer is displayed as a ribbon with F2 colored blue and F1 colored green. The fusion peptide (FP) is colored red and is shown with a transparent molecular surface. (b) Structures of RSV F protomers in the prefusion (left) and postfusion (right) conformations. Secondary structure elements that exist in substantially different orientations, conformations, or both are uniquely colored. The first 10 amino acids of the fusion peptide are not present in the postfusion structure.
Figure 2
Figure 2
Neutralizing epitopes on RSV F. For the pre- and postfusion RSV F trimers, a molecular surface is shown for two of the protomers, colored gray and white, whereas the third protomer is displayed as a green ribbon with residues that are displaced by more than 5 Å between the structures colored blue. Antigen-binding fragments (Fabs) for antibodies D25, motavizumab and 101F are shown as ribbons, with the heavy chains colored darker than the light chains.
See this image and copyright information in PMC

Similar articles

See all similar articles

Cited by

See all "Cited by" articles

References

    1. Hall CB, Simoes EA, Anderson LJ. Clinical and epidemiologic features of respiratory syncytial virus. Curr Top Microbiol Immunol. 2013;372:39–57. - PubMed
    1. Glezen WP, Taber LH, Frank AL, Kasel JA. Risk of primary infection and reinfection with respiratory syncytial virus. Am J Dis Child. 1986;140:543–546. - PubMed
    1. Hall CB. The burgeoning burden of respiratory syncytial virus among children. Infect Disord Drug Targets. 2012;12:92–97. - PubMed
    1. Hall CB, Weinberg GA, Blumkin AK, Edwards KM, Staat MA, Schultz AF, Poehling KA, Szilagyi PG, Griffin MR, Williams JV, et al. Respiratory syncytial virus-associated hospitalizations among children less than 24 months of age. Pediatrics. 2013;132:e341–348. - PubMed
    1. Lozano R, Naghavi M, Foreman K, Lim S, Shibuya K, Aboyans V, Abraham J, Adair T, Aggarwal R, Ahn SY, et al. Global and regional mortality from 235 causes of death for 20 age groups in 1990 and 2010: a systematic analysis for the Global Burden of Disease Study 2010. Lancet. 2013;380:2095–2128. - PMC - PubMed

Publication types

MeSH terms

Substances