Structure of the core ectodomain of the hepatitis C virus envelope glycoprotein 2

Nature

Volumn 509, Issue 7500, 2014, Pages 381-384

  Khan, Abdul Ghafoor ^a   Whidby, Jillian ^a   Miller, Matthew T ^a   Scarborough, Hannah ^b   Zatorski, Alexandra V ^a   Cygan, Alicja ^a   Price, Aryn A ^b   Yost, Samantha A ^a   Bohannon, Caitlin D ^b   Jacob, Joshy ^b   Grakoui, Arash ^b   Marcotrigiano, Joseph ^a  

^a RUTGERS UNIVERSITY   (United States)

^b EMORY UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CELL PROTEIN; CORE PROTEIN; GLYCOPROTEIN E2; HEPATITIS C VIRUS ENVELOPE GLYCOPROTEIN E2; IMMUNOGLOBULIN G; MEMBRANE FUSION PROTEIN; MONOCLONAL ANTIBODY; MONOCLONAL ANTIBODY 2A12; UNCLASSIFIED DRUG; VIRUS GLYCOPROTEIN;

ANTIBODY; DISEASE CONTROL; DISEASE PREVALENCE; HEPATITIS; HOST-PATHOGEN INTERACTION; MEDICINE; MOLECULAR ANALYSIS; PHYSIOLOGY; PROTEIN; VACCINE; VIRUS;

ALPHA HELIX; ANTIBODY PRODUCTION; ANTIGEN BINDING; ARTICLE; BETA SHEET; DEUTERIUM HYDROGEN EXCHANGE; DISULFIDE BOND; GEL PERMEATION CHROMATOGRAPHY; HEPATITIS C VIRUS; HYDROPHOBICITY; NONHUMAN; NUCLEOTIDE SEQUENCE; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN EXPRESSION; PROTEIN GLYCOSYLATION; PROTEIN PURIFICATION; PROTEIN STRUCTURE; VIRUS ENTRY; X RAY CRYSTALLOGRAPHY;

HEPATITIS C VIRUS;

CRYSTALLOGRAPHY, X-RAY; DISULFIDES; HEPACIVIRUS; HYDROGEN-ION CONCENTRATION; HYDROPHOBIC AND HYDROPHILIC INTERACTIONS; IMMUNOGLOBULIN FAB FRAGMENTS; IMMUNOGLOBULIN G; MODELS, MOLECULAR; PROTEIN FOLDING; PROTEIN STRUCTURE, TERTIARY; SCATTERING, SMALL ANGLE; SURFACE PROPERTIES; VIRAL ENVELOPE PROTEINS; VIRAL FUSION PROTEINS; VIRAL HEPATITIS VACCINES; VIRUS INTERNALIZATION;

EID: 84900798422     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature13117     Document Type: Article

References (43)

1. Lavanchy, D. Evolving epidemiology of hepatitis C virus. Clin. Microbiol. Infect. 17, 107-115 (2011).
2. Pileri, P. et al. Binding of hepatitis C virus to CD81. Science 282, 938-941 (1998).
3. Scarselli, E. et al. The human scavenger receptor class B type I is a novel candidate receptor for the hepatitis C virus. EMBO J. 21, 5017-5025 (2002).
4. Sautto, G., Tarr, A. W.,Mancini, N.&Clementi, M. Structural andantigenic definition of hepatitis C virus E2 glycoprotein epitopes targeted by monoclonal antibodies. Clin. Dev. Immunol. 2013, 450963 (2013).
5. Michalak, J. P. et al. Characterization of truncated forms of hepatitis C virus glycoproteins. J. Gen. Virol. 78, 2299-2306 (1997).
6. Drummer, H. E. & Poumbourios, P. Hepatitis C virus glycoprotein E2 contains a membrane-proximal heptad repeat sequence that is essential for E1E2 glycoprotein heterodimerization and viral entry. J. Biol. Chem. 279, 30066-30072 (2004).
7. Wahid, A. & Dubuisson, J. Virus-neutralizing antibodies to hepatitis C virus. J. Viral Hepat. 20, 369-376 (2013).
8. Keck, Z. Y. et al.Humanmonoclonal antibodies to a novel cluster of conformational epitopes on HCV E2 with resistance to neutralization escape in a genotype 2a isolate. PLoS Pathog. 8, e1002653 (2012).
9. Kong, L. et al. Structure of hepatitis C virus envelope glycoprotein E2 antigenic site 412 to 423 in complex with antibody AP33. J. Virol. 86, 13085-13088 (2012).
10. Kong, L. et al. Structural basis of hepatitis C virus neutralization by broadly neutralizing antibody HCV1. Proc. Natl Acad. Sci. USA 109, 9499-9504 (2012).
11. Deng, L. et al. Structural evidence for a bifurcated mode of action in the antibodymediated neutralization of hepatitis C virus. Proc. Natl Acad. Sci. USA 110, 7418-7422 (2013).
12. Whidby, J. et al. Blocking hepatitis C virus infection with recombinant form of envelope protein 2 ectodomain. J. Virol. 83, 11078-11089 (2009).
13. Krey, T. et al. The disulfide bonds in glycoprotein E2 of hepatitis C virus reveal the tertiary organization of the molecule. PLoS Pathog. 6, e1000762 (2010).
14. Keck, Z. Y. et al.Analysis of a highly flexible conformationalimmunogenicdomainA in hepatitis C virus E2. J. Virol. 79, 13199-13208 (2005).
15. Rothwangl, K. B.,Manicassamy, B., Uprichard, S. L.& Rong, L. Dissecting the role of putative CD81 binding regions of E2 in mediating HCV entry: putative CD81 binding region 1 is not involved in CD81 binding. Virol. J. 5, 46 (2008).
16. Lindenbach, B. D., Thiel, H.-J. & Rice, C. M. in Fields Virology (eds Knipe, D. M. & Howley, P. M.) 1101-1152 (Lippincott Williams & Wilkins, 2007).
17. White, J. M., Delos, S. E., Brecher, M. & Schornberg, K. Structures and mechanisms of viral membrane fusion proteins: multiple variations on a common theme. Crit. Rev. Biochem. Mol. Biol. 43, 189-219 (2008).
18. Vaney, M. C. & Rey, F. A. Class II enveloped viruses. Cell. Microbiol. 13, 1451-1459 (2011).
19. ElOmari, K., Iourin, O.,Harlos, K., Grimes, J. M.&Stuart, D. I. Structure of a pestivirus envelope glycoprotein E2 clarifies its role in cell entry. Cell Rep. 3, 30-35 (2013).
20. Li, Y.,Wang, J.,Kanai, R.&Modis, Y. Crystal structure of glycoproteinE2frombovine viral diarrhea virus. Proc. Natl Acad. Sci. USA 110, 6805-6810 (2013).
21. Forns, X. et al. Hepatitis C virus lacking the hypervariable region 1 of the second envelope protein is infectious and causes acute resolving or persistent infection in chimpanzees. Proc. Natl Acad. Sci. USA 97, 13318-13323 (2000).
22. Helle, F. et al. Role of N-linked glycans in the functions of hepatitis C virus envelope proteins incorporated into infectious virions. J. Virol. 84, 11905-11915 (2010).
23. Lavillette, D. et al. Characterization of fusion determinants points to the involvement of three discrete regions of both E1 and E2 glycoproteins in the membrane fusion process of hepatitis C virus. J. Virol. 81, 8752-8765 (2007).
24. Li, H. F., Huang, C. H., Ai, L. S., Chuang, C. K. & Chen, S. S. Mutagenesis of the fusion peptide-like domain of hepatitis C virus E1 glycoprotein: involvement in cell fusion and virus entry. J. Biomed. Sci. 16, 89 (2009).
25. Holm, L. & Rosenstrom, P. Dali server: conservation mapping in 3D. Nucleic Acids Res. 38, W545-W549 (2010).
26. Kong, L. et al. Hepatitis C virus E2 envelope glycoprotein core structure. Science 342, 1090-1094 (2013).
27. Reeves, P. J., Callewaert, N.,Contreras, R.&Khorana, H. G. Structure and functionin rhodopsin: high-level expression of rhodopsin with restricted and homogeneous N-glycosylation by a tetracycline-inducible N- acetylglucosaminyltransferase I-negative HEK293S stable mammalian cell line. Proc. Natl Acad. Sci. USA 99, 13419-13424 (2002).
28. Nielsen, S. S., Moller, M. & Gillilan, R. E. High-throughput biological small-angle X-ray scattering with a robotically loaded capillary cell. J. Appl. Crystallogr. 45, 213-223 (2012).
29. Petoukhov, M. V. et al. New developments in the ATSAS program package for small-angle scattering data analysis. J. Appl. Crystallogr. 45, 342-350 (2012).
30. Adams, P. D. et al. PHENIX: a comprehensive Python-based system for macromolecular structure solution. Acta Crystallogr. D 66, 213-221 (2010).
31. Emsley, P., Lohkamp, B., Scott, W. G. & Cowtan, K. Features and development of Coot. Acta Crystallogr. D 66, 486-501 (2010).
32. Murshudov, G. N. et al. REFMAC5 for the refinement of macromolecular crystal structures. Acta Crystallogr. D 67, 355-367 (2011).
33. Zhang, K. Y., Cowtan, K. & Main, P. Combining constraints for electron-density modification. Methods Enzymol. 277, 53-64 (1997).
34. Semenyuk, A. V. & Svergun, D. I. GNOM-a program package for small-angle scattering data processing. J. Appl. Crystallogr. 24, 537-540 (1991).
35. Svergun, D. I. Restoring low resolution structure of biological macromolecules from solution scattering using simulated annealing. Biophys. J. 76, 2879-2886 (1999).
36. Volkov, V. V. & Svergun, D. I. Uniqueness of ab initio shape determination in smallangle scattering. J. Appl. Crystallogr. 36, 860-864 (2003).
37. Kozin, M. B. & Svergun, D. Automated matching of high-and low-resolution structural models. J. Appl. Crystallogr. 34, 33-41 (2001).
38. Sharma, S. et al. Construct optimization for protein NMR structure analysis using amide hydrogen/deuteriumexchange mass spectrometry. Proteins 76, 882-894 (2009).
39. Tiller, T., Busse, C. E. & Wardemann, H. Cloning and expression ofmurine Ig genes from single B cells. J. Immunol. Methods 350, 183-193 (2009).
40. Mateu, G., Donis, R. O., Wakita, T., Bukh, J. & Grakoui, A. Intragenotypic JFH1 based recombinant hepatitis C virus produces high levels of infectious particles but causes increased cell death. Virology 376, 397-407 (2008).
41. Kabsch, W. & Sander, C. Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers 22, 2577-2637 (1983).
42. Katoh, K., Kuma, K., Toh, H.&Miyata, T.MAFFT version 5:improvement in accuracy of multiple sequence alignment. Nucleic Acids Res. 33, 511-518 (2005).
43. Waterhouse, A. M., Procter, J. B., Martin, D. M., Clamp, M. & Barton, G. J. Jalview Version 2-a multiple sequence alignment editor and analysis workbench. Bioinformatics 25, 1189-1191 (2009).