Cryo-EM structure of a native, fully glycosylated, cleaved HIV-1 envelope trimer

Science

Volumn 351, Issue 6277, 2016, Pages 1043-1048

  Lee, Jeong Hyun ^a   Ozorowski, Gabriel ^a   Ward, Andrew B ^a  

^a SCRIPPS RESEARCH INSTITUTE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CD4 ANTIGEN; EPITOPE; GLYCAN; GLYCOPROTEIN GP 120; GLYCOPROTEIN GP 140; GLYCOPROTEIN GP 41; N ACETYLGLUCOSAMINE; NEUTRALIZING ANTIBODY; PGT151 ANTIBODY; UNCLASSIFIED DRUG; VIRUS ENVELOPE GLYCOPROTEIN; VIRUS ENVELOPE PROTEIN; VIRUS GLYCOPROTEIN; MONOCLONAL ANTIBODY;

ANTIBODY; CELLS AND CELL COMPONENTS; CYTOLOGY; ELECTRON MICROSCOPY; HUMAN IMMUNODEFICIENCY VIRUS; HYDROPHOBICITY; MEMBRANE; NATIVE ELEMENT GROUP; RECONSTRUCTION; RESOLUTION; SOLUBILITY;

ALLOSTERISM; AMINO TERMINAL SEQUENCE; ANTIGEN BINDING; ARTICLE; BINDING SITE; CARBOXY TERMINAL SEQUENCE; CONFORMATIONAL TRANSITION; CRYOELECTRON MICROSCOPY; CRYSTAL STRUCTURE; DISULFIDE BOND; GENE MUTATION; GENOTYPE; HEAVY CHAIN; HUMAN IMMUNODEFICIENCY VIRUS 1; HYDROPHOBICITY; LIGHT CHAIN; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN CONFORMATION; PROTEIN CROSS LINKING; PROTEIN GLYCOSYLATION; PROTEIN PROTEIN INTERACTION; PROTEIN SECONDARY STRUCTURE; PROTEIN STABILITY; PROTEIN STRUCTURE; PROTEIN SYNTHESIS; STOICHIOMETRY; SURFACE PROPERTY; VIRUS STRAIN; AMINO ACID SEQUENCE; CHEMICAL PHENOMENA; CHEMISTRY; GENETICS; GLYCOSYLATION; HUMAN; IMMUNOLOGY; MOLECULAR GENETICS; PHYSIOLOGY; PROTEIN MULTIMERIZATION; PROTEIN TERTIARY STRUCTURE; ULTRASTRUCTURE; VIRUS ENTRY; X RAY CRYSTALLOGRAPHY;

CERCOPITHECINE HERPESVIRUS 1; HUMAN IMMUNODEFICIENCY VIRUS 1;

AMINO ACID SEQUENCE; ANTIBODIES, MONOCLONAL; ANTIBODIES, NEUTRALIZING; CRYSTALLOGRAPHY, X-RAY; GLYCOSYLATION; HIV ENVELOPE PROTEIN GP120; HIV ENVELOPE PROTEIN GP41; HIV-1; HUMANS; HYDROPHOBIC AND HYDROPHILIC INTERACTIONS; MOLECULAR SEQUENCE DATA; PROTEIN MULTIMERIZATION; PROTEIN STRUCTURE, TERTIARY; VIRUS INTERNALIZATION;

EID: 84961231130     PISSN: 00368075     EISSN: 10959203     Source Type: Journal    
DOI: 10.1126/science.aad2450     Document Type: Article

References (43)

1. J. Liu, A. Bartesaghi, M. J. Borgnia, G. Sapiro, S. Subramaniam, Nature 455, 109-113 (2008).
2. E. E. Tran et al., PLOS Pathog. 8, e1002797 (2012).
3. J. P. Julien et al., Proc. Natl. Acad. Sci. U.S.A. 110, 4351-4356 (2013).
4. J. P. Julien et al., Science 342, 1477-1483 (2013).
5. D. Lyumkis et al., Science 342, 1484-1490 (2013).
6. M. Pancera et al., Nature 514, 455-461 (2014).
7. Y. Do Kwon et al., Nat. Struct. Mol. Biol. 22, 522-531 (2015).
8. F. Garces et al., Immunity 43, 1053-1063 (2015).
9. J. H. Lee, N. de Val, D. Lyumkis, A. B. Ward, Structure 23, 1943-1951 (2015).
10. R. W. Sanders et al., PLOS Pathog. 9, e1003618 (2013).
11. R. W. Sanders et al., Science 349, aac4223 (2015).
12. P. Dosenovic et al., Cell 161, 1505-1515 (2015).
13. J. Chen et al., Science 349, 191-195 (2015).
14. L. G. Abrahamyan et al., J. Virol. 79, 106-115 (2005).
15. Z. Y. Sun et al., J. Mol. Biol. 426, 1095-1108 (2014).
16. C. Blattner et al., Immunity 40, 669-680 (2014).
17. J. B. Munro et al., Science 346, 759-763 (2014).
18. P. Pugach et al., J. Virol. 89, 3380-3395 (2015).
19. J. P. Julien et al., Proc. Natl. Acad. Sci. U.S.A. 112, 11947-11952 (2015).
20. R. W. Sanders et al., J. Virol. 76, 8875-8889 (2002).
21. M. Guttman et al., Structure 22, 974-984 (2014).
22. J. Huang et al., Nature 491, 406-412 (2012).
23. R. Pejchal et al., J. Virol. 83, 8451-8462 (2009).
24. S. Bryson, J. P. Julien, R. C. Hynes, E. F. Pai, J. Virol. 83, 11862-11875 (2009).
25. I. A. Wilson, J. J. Skehel, D. C. Wiley, Nature 289, 366-373 (1981).
26. E. Falkowska et al., Immunity 40, 657-668 (2014).
27. F. Garces et al., Cell 159, 69-79 (2014).
28. D. Sok et al., Sci. Transl. Med. 6, 236ra63 (2014).
29. J. H. Lee et al., Nat. Commun. 6, 8167 (2015).
30. R. Derking et al., PLOS Pathog. 11, e1004767 (2015).
31. L. K. Pritchard et al., J. Virol. 89, 6952-6959 (2015).
32. J. Huang et al., Nature 515, 138-142 (2014).
33. A. S. Kim, D. P. Leaman, M. B. Zwick, PLOS Pathog. 10, e1004271 (2014).
34. J. M. Cutalo, L. J. Deterding, K. B. Tomer, J. Am. Soc. Mass Spectrom. 15, 1545-1555 (2004).
35. E. P. Go et al., J. Virol. 89, 8245-8257 (2015).
36. E. P. Go et al., J. Virol. 85, 8270-8284 (2011).
37. E. T. Crooks et al., Hum. Antibodies 14, 101-113 (2005).
38. R. M. Cardoso et al., Immunity 22, 163-173 (2005).
39. G. Frey et al., Proc. Natl. Acad. Sci. U.S.A. 105, 3739-3744 (2008).
40. D. P. Leaman, J. H. Lee, A. B. Ward, M. B. Zwick, J. Virol. 89, 6725-6745 (2015).
41. J. Chen et al., J. Virol. 88, 1249-1258 (2014).
42. J. Guenaga et al., PLOS ONE 6, e16074 (2011).
43. G. Ofek et al., Proc. Natl. Acad. Sci. U.S.A. 107, 17880-17887 (2010).