Structure of RSV Fusion Glycoprotein Trimer Bound to a Prefusion-Specific Neutralizing Antibody
Open accessAbstract
Building Better Vaccines: Vaccines are one of the most effective tools to protect against infectious diseases. Unfortunately, vaccines for diseases with the highest global health burdens, such as HIV, malaria, and tuberculosis, are not yet available. Koff et al. (p. 1064 ) review the latest advances in vaccine development and why these particular diseases remain such a challenge. Respiratory syncytial virus (RSV) is a serious cause of morbidity and mortality in infants and young children worldwide. Although a prophylactic antibody is available for children at high risk, a vaccine is much needed. As a potential step toward this goal, McLellan et al. (p. 1113 , published online 25 April) solved the cocrystal structure of a neutralizing antibody (D25) bound to the prefusion F protein of RSV. Knowledge of the structure of the prefusion protein should help to guide vaccine design and the development of additional therapeutics.
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Newfound structural insights into F protein conformation have revealed that vaccinating against the prefusion conformation elicits superior neutralizing antibody response.
“Although some candidates have failed clinical trials owing to insufficient neutralizing antibody titres174, newfound structural insights into F protein conformation have revealed that vaccinating against the prefusion conformation elicits superior neutralizing antibody response175–178.”
From mRNA vaccines for infectious diseases: principles, delivery and clinical translation (2021) · cites this paper as [176]
Antibodies 5C4, AM22, and D25 are substantially more potent than palivizumab and target antigenic site Ø.
“Antibodies such as 5C4 (7), AM22, and D25 (11, 12) are substantially more potent than palivizumab and target antigenic site Ø, a metastable site located at the membrane-distal apex of the prefusion RSV F trimer (7).”
From Structure-Based Design of a Fusion Glycoprotein Vaccine for Respiratory Syncytial Virus (2013) · cites this paper as [7]
The β-carbons of serine residues 155 and 290 are 4.4 Å apart in the D25-bound RSV F structure and 124.2 Å apart in the postfusion structure.
“The β-carbons of serine residues 155 and 290 are 4.4 Å apart in the D25-bound RSV F structure (7) and 124.2 Å apart in the postfusion structure (5) (Fig. 1 and fig. S2).”
From Structure-Based Design of a Fusion Glycoprotein Vaccine for Respiratory Syncytial Virus (2013) · cites this paper as [7]
Antigenic site Ø is a metastable site specific to the prefusion state of RSV F and is targeted by extremely potent RSV-neutralizing antibodies.
“focused on antigenic site Ø, a metastable site specific to the prefusion state of the RSV fusion (F) glycoprotein, as this site is targeted by extremely potent RSV-neutralizing antibodies.”
From Structure-Based Design of a Fusion Glycoprotein Vaccine for Respiratory Syncytial Virus (2013) · cites this paper as [7]
The steep slope of this correlation likely reflects the substantially higher neutralization potency observed for prefusion-specific antibodies that target antigenic site Ø.
“Notably, the steep slope of this correlation likely reflects the substantially higher neutralization potency observed for prefusion-specific antibodies that target antigenic site Ø (7, 38).”
From Structure-Based Design of a Fusion Glycoprotein Vaccine for Respiratory Syncytial Virus (2013) · cites this paper as [7]
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- Authors
- McLellan, J. S., Chen, M., Leung, S., Graepel, K. W., Du, X., Yang, Y., Zhou, T., Baxa, U., Yasuda, E., Beaumont, T., Kumar, A., Modjarrad, K., Zheng, Z., Zhao, M., Xia, N., Kwong, P. D., & Graham, B. S.
- Affiliations
- National Institutes of Health (US)
- Frederick National Laboratory for Cancer Research (US)
- Amsterdam UMC Location University of Amsterdam (NL)
- Xiamen University (CN)
- Corresponding author
- McLellan, Jason S.
- Kwong, Peter D.
- ORCID
- Venue
- Science
- Published
- 2013-05-31
- Volume
- 340
- Issue
- 6136
- Pages
- 1113-1117
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- PMC
- PMC4459498
- OpenAlex
- W2043056303
- Cited by
- 883
- References
- 51
- Citations by year
- 2026: 83 · 2025: 68 · 2024: 86 · 2023: 79 · 2022: 62 · 2021: 80 · 2020: 59 · 2019: 68 · 2018: 52 · 2017: 59 · 2016: 59 · 2015: 62 · 2014: 40 · 2013: 26
- FWCI
- 45.42
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Science (publishedVersion)
- PubMed (publishedVersion)
- Pure Amsterdam UMC (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institutes of Health
- National Institute of Allergy and Infectious Diseases (ZIAAI005061, ZIAAI005024)
- Topics
- Health Sciences › Medicine › Epidemiology › Respiratory viral infections research
- Health Sciences › Medicine › Infectious Diseases › SARS-CoV-2 and COVID-19 Research
- Health Sciences › Medicine › Epidemiology › Virology and Viral Diseases
- Keywords
- respiratory syncytial virus, F glycoprotein, neutralizing antibodies, immune complexes, co-crystal structure, antigenic determinants, palivizumab, vaccine design
- MeSH terms
- Palivizumab, Amino Acid Sequence, Animals, Female, Glycoproteins, Humans, Mice, Inbred BALB C, Molecular Sequence Data, Neutralization Tests, Protein Conformation, Respiratory Syncytial Viruses, Viral Fusion Proteins, Crystallography, X-Ray, Respiratory Syncytial Virus Vaccines, Mice, Virus Internalization, Protein Multimerization, Antibodies, Neutralizing, HEK293 Cells, Antibodies, Monoclonal, Humanized
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