Structure of RSV fusion glycoprotein trimer bound to a prefusion-specific neutralizing antibody

Science

Volumn 340, Issue 6136, 2013, Pages 1113-1117

  McLellan, Jason S ^a   Chen, Man ^a   Leung, Sherman ^a   Graepel, Kevin W ^a   Du, Xiulian ^a   Yang, Yongping ^a   Zhou, Tongqing ^a   Baxa, Ulrich ^b   Yasuda, Etsuko ^c   Beaumont, Tim ^c   Kumar, Azad ^a   Modjarrad, Kayvon ^a   Zheng, Zizheng ^d   Zhao, Min ^d   Xia, Ningshao ^d   Kwong, Peter D ^a   Graham, Barney S ^a  

^a NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES   (United States)

^b SAIC FREDERICK INC   (United States)

^c ACADEMIC MEDICAL CENTER   (Netherlands)

^d XIAMEN UNIVERSITY   (China)

Author keywords

[No Author keywords available]

Indexed keywords

GLYCOPROTEIN; MOTAVIZUMAB; NEUTRALIZING ANTIBODY; PALIVIZUMAB; RESPIRATORY SYNCYTIAL PNEUMOVIRUS PROTEIN; UNCLASSIFIED DRUG; VIRUS PROTEIN;

ANTIBODY; ANTIGEN; CRYSTAL STRUCTURE; DISEASE CONTROL; ELECTRON MICROSCOPY; PROTEIN; PUBLIC HEALTH; VACCINE;

ANTIGEN BINDING; ARTICLE; CONFORMATIONAL TRANSITION; CRYSTAL STRUCTURE; DISULFIDE BOND; GLYCOSYLATION; HYDROGEN BOND; MOLECULAR RECOGNITION; NONHUMAN; PH; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN SECONDARY STRUCTURE; PROTEIN STRUCTURE; X RAY DIFFRACTION;

RESPIRATORY SYNCYTIAL VIRUS; RICE STRIPE VIRUS;

EID: 84878349946     PISSN: 00368075     EISSN: 10959203     Source Type: Journal    
DOI: 10.1126/science.1234914     Document Type: Article

References (40)

1. W. P. Glezen, L. H. Taber, A. L. Frank, J. A. Kasel, Am. J. Dis. Child. 140, 543 (1986).
2. D. K. Shay et al., JAMA 282, 1440 (1999).
3. C. B. Hall et al., N. Engl. J. Med. 360, 588 (2009).
4. R. Lozano et al., Lancet 380, 2095 (2012).
5. S. Johnson et al., J. Infect. Dis. 176, 1215 (1997).
6. J. A. Beeler, K. van Wyke Coelingh, J. Virol. 63, 2941 (1989).
7. The IMpact-RSV Study Group, Pediatrics 102, 531 (1998).
8. E. J. Collarini et al., J. Immunol. 183, 6338 (2009).
9. H. Wu et al., J. Mol. Biol. 368, 652 (2007).
10. M. J. Kwakkenbos et al., Nat. Med. 16, 123 (2010).
11. B. S. Graham, Immunol. Rev. 239, 149 (2011).
12. E. E. Walsh, J. Hruska, J. Virol. 47, 171 (1983).
13. J. Arbiza et al., J. Gen. Virol. 73, 2225 (1992).
14. J. A. López et al., J. Virol. 72, 6922 (1998).
15. J. A. López, C. Peñas, B. García-Barreno, J. A. Melero, A. Portela, J. Virol. 64, 927 (1990).
16. J. S. McLellan, Y. Yang, B. S. Graham, P. D. Kwong, J. Virol. 85, 7788 (2011).
17. K. A. Swanson et al., Proc. Natl. Acad. Sci. U.S.A. 108, 9619 (2011).
18. M. Magro et al ., Proc. Natl. Acad. Sci. U.S.A. 109, 3089 (2012).
19. Information on materials and methods is available on Science Online.
20. H. Spits, T. Beaumont, RSV-specific binding molecules and means for producing them. Patent Application 12/600,950 (2010).
21. T. Beaumont, A. Q. Bakker, E. Yasuda, RSV specific binding molecule. Patent application 12/898,325 (2012).
22. Approximately 100-fold greater potency of AM22 and D25 relative to palivizumab was observed by Beaumont and colleagues in a plaque assay; in our flow-based neutralization assay, we observed a 15-fold improvement over palivizumab and a 3-fold improvement over motavizumab.
23. M. Pancera et al., PLoS ONE 8, e55701 (2013).
24. S. Frank et al., J. Mol. Biol. 308, 1081 (2001).
25. S. Chaiwatpongsakorn, R. F. Epand, P. L. Collins, R. M. Epand, M. E. Peeples, J. Virol. 85, 3968 (2011).
26. B. D. Welch et al., Proc. Natl. Acad. Sci. U.S.A. 109, 16672 (2012).
27. H. S. Yin, X. Wen, R. G. Paterson, R. A. Lamb, T. S. Jardetzky, Nature 439, 38 (2006).
28. J. S. McLellan et al., Nat. Struct. Mol. Biol. 17, 248 (2010).
29. RSV F has the shortest fusion peptide of all paramyxoviruses, which may allow it to move from an initially exposed position to the central cavity of the trimer.
30. J. E. Lee et al ., Nature 454, 177 (2008).
31. I. A. Wilson, J. J. Skehel, D. C. Wiley, Nature 289, 366 (1981).
32. The fusion peptide is connected to the surface-exposed α2 and α3 helices through a cylindrical opening between the protomers that is roughly 10 Å in diameter; this opening may be used as an exit path for the fusion peptide during triggering.
33. X. Wen et al., Nat. Struct. Mol. Biol. 19, 461 (2012).
34. 1 residues 461 to 513 move at least 8 Å, which could destabilize the fusion peptide and lead to triggering.
35. P. Chambers, C. R. Pringle, A. J. Easton, J. Gen. Virol. 73, 1717 (1992).
36. 1 residues 205 to 225 could elicit neutralizing activity in rabbits, although a specific epitope was not defined (39).
37. D. C. Ekiert et al., Nature 489, 526 (2012).
38. A. L. Connor, D. J. Bevitt, G. L. Toms, J. Med. Virol. 63, 168 (2001).
39. C. Corvaisier, C. Bourgeois, P. Pothier, Arch. Virol. 142, 1073 (1997).
40. H. Ashkenazy, E. Erez, E. Martz, T. Pupko, N. Ben-Tal, Nucleic Acids Res. 38, (Web Server), W529 (2010).