Crystal structure of glycoprotein E2 from bovine viral diarrhea virus

Proceedings of the National Academy of Sciences of the United States of America

Volumn 110, Issue 17, 2013, Pages 6805-6810

  Li, Yue ^a   Wang, Jimin ^a   Kanai, Ryuta ^a,b   Modis, Yorgo ^a  

^a YALE UNIVERSITY   (United States)

^b UNIVERSITY OF TOKYO   (Japan)

Author keywords

Domain swap; Family Flaviviridae; Fusion motif; Genus hepacivirus; PH sensing

Indexed keywords

GLYCOPROTEIN E2;

ARTICLE; BOVINE DIARRHEA VIRUS; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; CRYSTAL STRUCTURE; DISULFIDE BOND; NONHUMAN; PRIORITY JOURNAL; PROTEIN MOTIF;

AMINO ACID SEQUENCE; CRYSTALLOGRAPHY, X-RAY; DIARRHEA VIRUS 1, BOVINE VIRAL; EPITOPE MAPPING; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN CONFORMATION; VIRAL ENVELOPE PROTEINS; VIRUS INTERNALIZATION;

ANIMALIA; BOVINE VIRAL DIARRHEA VIRUS 1; FLAVIVIRIDAE; HEPACIVIRUS; HEPATITIS C VIRUS; PESTIVIRUS;

EID: 84876865608     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1300524110     Document Type: Article

References (45)

1. Lindenbach BD, Thiel H-J, Rice CM (2007) Flaviviridae: The viruses and their replication. Fields Virology, eds Knipe DM, Howley PM (Lippincott Williams and Wilkins, Philadelphia), 5th Ed, pp 1102-1152.
2. Shepard CW, Finelli L, Alter MJ (2005) Global epidemiology of hepatitis C virus infection. Lancet Infect Dis 5(9):558-567.
3. Gastaminza P, et al. (2010) Ultrastructural and biophysical characterization of hepatitis C virus particles produced in cell culture. J Virol 84(21):10999-11009.
4. Wegelt A, Reimann I, Granzow H, Beer M (2011) Characterization and purification of recombinant bovine viral diarrhea virus particles with epitope-tagged envelope proteins. J Gen Virol 92(Pt 6):1352-1357.
5. Yu X, et al. (2007) Cryo-electron microscopy and three-dimensional reconstructions of hepatitis C virus particles. Virology 367(1):126-134.
6. Krey T, Thiel HJ, Rümenapf T (2005) Acid-resistant bovine pestivirus requires activation for pH-triggered fusion during entry. J Virol 79(7):4191-4200.
7. Meertens L, Bertaux C, Dragic T (2006) Hepatitis C virus entry requires a critical postinternalization step and delivery to early endosomes via clathrin-coated vesicles. J Virol 80(23):11571-11578.
8. Krey T, et al. (2006) Function of bovine CD46 as a cellular receptor for bovine viral diarrhea virus is determined by complement control protein 1. J Virol 80(8): 3912-3922.
9. Petracca R, et al. (2000) Structure-function analysis of hepatitis C virus envelope-CD81 binding. J Virol 74(10):4824-4830.
10. Tscherne DM, Evans MJ, Macdonald MR, Rice CM (2008) Transdominant inhibition of bovine viral diarrhea virus entry. J Virol 82(5):2427-2436.
11. von Hahn T, Rice CM (2008) Hepatitis C virus entry. J Biol Chem 283(7):3689-3693.
12. Tscherne DM, et al. (2006) Time-and temperature-dependent activation of hepatitis C virus for low-pH-triggered entry. J Virol 80(4):1734-1741.
13. Mathapati BS, et al. (2010) Entry of bovine viral diarrhea virus into ovine cells occurs through clathrin-dependent endocytosis and low pH-dependent fusion. In Vitro Cell Dev Biol Anim 46(5):403-407.
14. Campos SK, Chapman JA, Deymier MJ, Bronnimann MP, Ozbun MA (2012) Opposing effects of bacitracin on human papillomavirus type 16 infection: Enhancement of binding and entry and inhibition of endosomal penetration. J Virol 86(8):4169-4181.
15. Li X, et al. (2011) Identification of host cell binding peptide from an overlapping peptide library for inhibition of classical swine fever virus infection. Virus Genes 43(1):33-40.
16. Liang D, et al. (2003) The envelope glycoprotein E2 is a determinant of cell culture tropism in ruminant pestiviruses. J Gen Virol 84(Pt 5):1269-1274.
17. Pileri P, et al. (1998) Binding of hepatitis C virus to CD81. Science 282(5390):938-941.
18. Hadlock KG, et al. (2000) Human monoclonal antibodies that inhibit binding of hepatitis C virus E2 protein to CD81 and recognize conserved conformational epi-topes. J Virol 74(22):10407-10416.
19. Weiland E, et al. (1990) Pestivirus glycoprotein which induces neutralizing antibodies forms part of a disulfide-linked heterodimer. J Virol 64(8):3563-3569.
20. Rümenapf T, Unger G, Strauss JH, Thiel HJ (1993) Processing of the envelope glyco-proteins of pestiviruses. J Virol 67(6):3288-3294.
21. Thiel HJ, Stark R, Weiland E, Rümenapf T, Meyers G (1991) Hog cholera virus: Molecular composition of virions from a pestivirus. J Virol 65(9):4705-4712.
22. Ronecker S, Zimmer G, Herrler G, Greiser-Wilke I, Grummer B (2008) Formation of bovine viral diarrhea virus E1-E2 heterodimers is essential for virus entry and depends on charged residues in the transmembrane domains. J Gen Virol 89(Pt 9):2114-2121.
23. Patel J, Patel AH, McLauchlan J (2001) The transmembrane domain of the hepatitis C virus E2 glycoprotein is required for correct folding of the E1 glycoprotein and native complex formation. Virology 279(1):58-68.
24. Fritz R, Stiasny K, Heinz FX (2008) Identification of specific histidines as pH sensors in flavivirus membrane fusion. J Cell Biol 183(2):353-361.
25. Nayak V, et al. (2009) Crystal structure of dengue virus type 1 envelope protein in the postfusion conformation and its implications for membrane fusion. J Virol 83(9):4338-4344.
26. Qin ZL, Zheng Y, Kielian M (2009) Role of conserved histidine residues in the low-pH dependence of the Semliki Forest virus fusion protein. J Virol 83(9):4670-4677.
27. Zheng Y, Sánchez-San Martín C, Qin ZL, Kielian M (2011) The domain I-domain III linker plays an important role in the fusogenic conformational change of the al-phavirus membrane fusion protein. J Virol 85(13):6334-6342.
28. de Boer SM, et al. (2012) Acid-activated structural reorganization of the Rift Valley fever virus Gc fusion protein. J Virol 86(24):13642-13652.
29. Dessau M, Modis Y (2013) Crystal structure of glycoprotein C from Rift Valley fever virus. Proc Natl Acad Sci USA 110(5):1696-1701.
30. Holm L, Rosenström P (2010) Dali server: Conservation mapping in 3D. Nucleic Acids Res 38(Web Server issue):W545-9.
31. Krey T, et al. (2010) The disulfide bonds in glycoprotein E2 of hepatitis C virus reveal the tertiary organization of the molecule. PLoS Pathog 6(2):e1000762.
32. Vieyres G, et al. (2010) Characterization of the envelope glycoproteins associated with infectious hepatitis C virus. J Virol 84:10159-10168.
33. Modis Y, Ogata S, Clements D, Harrison SC (2004) Structure of the dengue virus envelope protein after membrane fusion. Nature 427(6972):313-319.
34. van Rijn PA, Miedema GK, Wensvoort G, van Gennip HG, Moormann RJ (1994) An-tigenic structure of envelope glycoprotein E1 of hog cholera virus. J Virol 68(6): 3934-3942.
35. Garry RF, Dash S (2003) Proteomics computational analyses suggest that hepatitis C virus E1 and pestivirus E2 envelope glycoproteins are truncated class II fusion proteins. Virology 307(2):255-265.
36. Boo I, et al. (2012) Distinct roles in folding, CD81 receptor binding and viral entry for conserved histidine residues of hepatitis C virus glycoprotein E1 and E2. Biochem J 443 (1):85-94.
37. Drummer HE, Boo I, Poumbourios P (2007) Mutagenesis of a conserved fusion pep-tide-like motif and membrane-proximal heptad-repeat region of hepatitis C virus glycoprotein E1. J Gen Virol 88(Pt 4):1144-1148.
38. Wallin M, Ekström M, Garoff H (2004) Isomerization of the intersubunit disulphide-bond in Env controls retrovirus fusion. EMBO J 23(1):54-65.
39. El Omari K, Iourin O, Harlos K, Grimes JM, Stuart DI (2013) Structure of a pestivirus envelope glycoprotein E2 clarifies its role in cell entry. Cell Rep 3(1):30-35.
40. Kabsch W (2010) Xds. Acta Crystallogr D Biol Crystallogr 66(Pt 2):125-132.
41. Adams PD, et al. (2011) The Phenix software for automated determination of mac-romolecular structures. Methods 55(1):94-106.
42. Rould MA, Perona JJ, Steitz TA (1992) Improving multiple isomorphous replacement phasing by heavy-atom refinement using solvent-flattened phases. Acta Crystallogr A 48(Pt 5):751-756.
43. Cowtan K (2010) Recent developments in classical density modification. Acta Crys-tallogr D Biol Crystallogr 66(Pt 4):470-478.
44. Emsley P, Cowtan K (2004) Coot: Model-building tools for molecular graphics. Acta Crystallogr D Biol Crystallogr 60(Pt 12 Pt 1):2126-2132.
45. Murshudov GN, Vagin AA, Dodson EJ (1997) Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr D Biol Crystallogr 53(Pt 3):240-255.