7LVW
Structure of RSV F in Complex with VHH Cl184
Summary for 7LVW
| Entry DOI | 10.2210/pdb7lvw/pdb |
| Related | 7LVU |
| Descriptor | Fusion glycoprotein F0, F-VHH-Cl184, beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (6 entities in total) |
| Functional Keywords | nanobody, vhh, antibody, fusion protein, virus complex, immune system, immune system-viral protein complex, immune system/viral protein |
| Biological source | Respiratory syncytial virus More |
| Total number of polymer chains | 12 |
| Total formula weight | 434735.02 |
| Authors | Hsieh, C.-L.,McLellan, J.S. (deposition date: 2021-02-26, release date: 2021-03-24, Last modification date: 2024-10-30) |
| Primary citation | Rossey, I.,Hsieh, C.L.,Sedeyn, K.,Ballegeer, M.,Schepens, B.,Mclellan, J.S.,Saelens, X. A vulnerable, membrane-proximal site in human respiratory syncytial virus F revealed by a prefusion-specific single-domain antibody. J.Virol., 95:-, 2021 Cited by PubMed Abstract: Human respiratory syncytial virus (RSV) is a major cause of lower respiratory tract disease, especially in young children and the elderly. The fusion protein (F) exists in a pre- and postfusion conformation and is the main target of RSV-neutralizing antibodies. Highly potent RSV-neutralizing antibodies typically bind sites that are unique to the prefusion conformation of F. In this study we screened a single-domain antibody (VHH) library derived from a llama immunized with prefusion-stabilized F and identified a prefusion F-specific VHH that can neutralize RSV A at subnanomolar concentrations. Structural analysis revealed that this VHH primarily binds to antigenic site I while also making contacts with residues in antigenic site III and IV. This new VHH reveals a previously underappreciated membrane-proximal region sensitive for neutralization.RSV is an important respiratory pathogen. This study describes a prefusion F-specific VHH that primarily binds to antigenic site I of RSV F. This is the first time that a prefusion F-specific antibody that binds this site is reported. In general, antibodies that bind to site I are poorly neutralizing, whereas the VHH described here neutralizes RSV A at subnanomolar concentrations. Our findings contribute to insights into the RSV F antigenic map. PubMed: 33692208DOI: 10.1128/JVI.02279-20 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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