Glycosylation site alteration in the evolution of influenza a (H1N1) viruses

PLoS ONE

Volumn 6, Issue 7, 2011, Pages

  Sun, Shisheng ^a   Wang, Qinzhe ^a   Zhao, Fei ^a   Chen, Wentian ^a   Li, Zheng ^a  

^a NORTHWEST UNIVERSITY   (China)

Author keywords

[No Author keywords available]

Indexed keywords

INFLUENZA VIRUS HEMAGGLUTININ; VIRUS SIALIDASE; HEMAGGLUTININ, HUMAN INFLUENZA A VIRUS; SIALIDASE;

AMINO ACID SEQUENCE; ARTICLE; CONTROLLED STUDY; INFLUENZA VIRUS A H1N1; MOLECULAR EVOLUTION; MOLECULAR MODEL; NONHUMAN; PREDICTION; PROTEIN GLYCOSYLATION; PROTEIN STRUCTURE; CHEMICAL STRUCTURE; GLYCOSYLATION; HUMAN; INFLUENZA; METABOLISM; PHYLOGENY; PHYSIOLOGY; PROTEIN CONFORMATION; VIROLOGY; VIRUS GENOME;

HUMAN INFLUENZA VIRUS; INFLUENZA A VIRUS; ORTHOMYXOVIRIDAE;

EVOLUTION, MOLECULAR; GENOME, VIRAL; GLYCOSYLATION; HEMAGGLUTININ GLYCOPROTEINS, INFLUENZA VIRUS; HUMANS; INFLUENZA A VIRUS, H1N1 SUBTYPE; INFLUENZA, HUMAN; MODELS, MOLECULAR; NEURAMINIDASE; PHYLOGENY; PROTEIN CONFORMATION;

EID: 79960872741     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0022844     Document Type: Article

References (50)

1. Neumann G, Noda T, Kawaoka Y, (2009) Emergence and pandemic potential of swine-origin H1N1 influenza virus. Nature 459: 931-939.
2. Stevens J, Corper AL, Basler CF, Taubenberger JK, Palese P, et al. (2004) Structure of the uncleaved human H1 hemagglutinin from the extinct 1918 influenza virus. Science 303: 1866-1870.
3. Johnson NPAS, Mueller J, (2002) Updating the accounts: global mortality of the 1918-1920 "spanish" influenza pandemic. B Hist Med 76: 105-115.
4. Kilbourne ED, (2006) Influenza pandemics of the 20th century. Emerg Infect Dis 12: 9-14.
5. Zimmer SM, Burke DS, (2009) Historical perspective- emergence of influenza A (H1N1) viruses. New Engl J Med 361: 279-285.
6. Zhirnov OP, Vorobjeva IV, Saphonova OA, Poyarkov SV, Ovcharenko AV, et al. (2009) Structural and evolutionary characteristics of HA, NA, NS and M genes of clinical influenza A/H3N2 viruses passaged in human and canine cells. J Clin Virol 45: 322-333.
7. Blake TA, Williams TL, Pirkle JL, Barr JR, (2009) Targeted N-Linked glycosylation analysis of H5N1 influenza hemagglutinin by selective sample preparation and liquid chromatography/tandem mass spectrometry. Anal Chem 81: 3109-3118.
8. Schulze IT, (1997) Effects of glycosylation on the properties and functions of influenza virus hemagglutinin. J Infect Dis 176 (Suppl 1): S24-28.
9. Gambaryan AS, Marinina VP, Tuzikov AB, Bovin NV, Rudneva IA, et al. (1998) Effects of host-dependent glycosylation of hemagglutinin on receptor-binding properties of H1N1 human influenza A virus grown in MDCK cells and in embryonated eggs. Virology 247: 170-177.
10. Gao Y, Zhang Y, Shinya K, Deng G, Jiang Y, et al. (2009) Identification of amino acids in HA and PB2 critical for the transmission of H5N1 avian influenza viruses in a mammalian host. PLoS Pathog 5: e1000709.
11. Matrosovich M, Zhou N, Kawaoka Y, Webster R, (1999) The surface glycoproteins of H5 influenza viruses isolated from humans, chickens, and wild aquatic birds have distinguishable properties. J Virol 73: 1146-1155.
12. Ohuchi M, Ohuchi R, Feldmann A, Klenk H, (1997) Regulation of receptor binding affinity of influenza virus hemagglutinin by its carbohydrate moiety. J Virol 71: 8377-8384.
13. Mishin VP, Novikov D, Hayden FG, Gubareva LV, (2005) Effect of hemagglutinin glycosylation on influenza virus susceptibility to neuraminidase inhibitors. J Virol 79: 12416-12424.
14. Abe Y, Takashita E, Sugawara K, Matsuzaki Y, Muraki Y, et al. (2004) Effect of the addition of oligosaccharides on the biological activities and antigenicity of influenza A/H3N2 virus hemagglutinin. J Virol 78: 9605-9611.
15. Munk K, Pritzer E, Kretzschmar E, Gutte B, Garten W, et al. (1992) Carbohydrate masking of an antigenic epitope of influenza virus haemagglutinin independent of oligosaccharide size. Glycobiology 2: 233-240.
16. Wang C-C, Chen J-R, Tseng Y-C, Hsu C-H, Hung Y-F, et al. (2009) Glycans on influenza hemagglutinin affect receptor binding and immune response. Proc Natl Acad Sci U S A 106: 18137-18142.
17. Das SR, Puigbo P, Hensley SE, Hurt DE, Bennink JR, et al. (2010) Glycosylation Focuses Sequence Variation in the Influenza A Virus H1 Hemagglutinin Globular Domain. PLOS pathogens 6: e1001211.
18. Deshpande KL, Fried VA, Ando M, Webster RG, (1987) Glycosylation affects cleavage of an H5N2 influenza virus hemagglutinin and regulates virulence. Proc Natl Acad Sci U S A 84: 36-40.
19. Ohuchi M, Orlich M, Ohuchi R, Simpson BEJ, Garten W, et al. (1989) Mutations at the cleavage site of the hemagglutinin alter the pathogenicity of influenza virus a/chick/penn/83 (H5N2). Virology 168: 274-280.
20. Bosch FX, Garten W, Klenk H-D, Rott R, (1981) Proteolytic cleavage of influenza virus hemagglutinins: primary structure of the connecting peptide between HA1 and HA2 determines proteolytic cleavability and pathogenicity of avian influenza viruses. Virology 113: 725-735.
21. Matsuoka Y, Swayne DE, Thomas C, Rameix-Welti M-A, Naffakh N, et al. (2009) Neuraminidase stalk length and additional glycosylation of the hemagglutinin influence the virulence of influenza H5N1 viruses for mice. J Virol 83: 4704-4708.
22. Wu ZL, Ethen C, Hickey GE, Jiang W, (2009) Active 1918 pandemic flu viral neuraminidase has distinct N-glycan profile and is resistant to trypsin digestion. Biochem Bioph Res Co 379: 749-753.
23. Bause E, (1983) Structural requirements of N-glycosylation of proteins. Studies with proline peptides as conformational probes. Biochem J 209: 331-336.
24. Zhang H, Loriaux P, Eng J, Campbell D, Keller A, et al. (2006) UniPep- a database for human N- linked glycosites: a resource for biomarker discovery. Genome Biology 7: R73.
25. Zhang M, Gaschen B, Blay W, Foley B, Haigwood N, et al. (2004) Tracking global patterns of N-linked glycosylation site variation in highly variable viral glycoproteins: HIV, SIV, and HCV envelopes and influenza hemagglutinin. Glycobiology 14: 1229-1246.
26. Wei C-J, Boyington JC, Dai K, Houser KV, Pearce MB, et al. (2010) Cross-neutralization of 1918 and 2009 influenza viruses: role of glycans in viral evolution and vaccine design. Sci Transl Med 2: 24ra21.
27. Igarashi M, Ito K, Kida H, Takada A, (2008) Genetically destined potentials for N-linked glycosylation of influenza virus hemagglutinin. Virology 376: 323-329.
28. Hancock K, Veguilla V, Lu X, Zhong W, Butler EN, et al. (2009) Cross-reactive antibody responses to the 2009 pandemic H1N1 influenza virus. New Engl J Med 361: 1945-1952.
29. Vigerust DJ, Shepherd VL, (2007) Virus glycosylation: role in virulence and immune interactions. TRENDS Microbiol 15: 211-218.
30. Chang S, Zhang J, Liao X, Zhu X, Wang D, et al. (2007) Influenza Virus Database (IVDB): an integrated information resource and analysis platform for influenza virus research. Nucleic Acids Res 35: D376-D380.
31. Bao Y, Bolotov P, Dernovoy D, Kiryutin B, Zaslavsky L, et al. (2008) The influenza virus resource at the national center for biotechnology information. J Virol 82: 596-601.
32. Arnold K, Bordoli L, Kopp J, Schwede T, (2006) The SWISS-MODEL workspace: A web-based environment for protein structure homology modelling. Bioinformatics 22: 195-201.
33. Bohne-Lang A, Lieth C-Wvd, (2005) GlyProt: in silico glycosylation of proteins. Nucleic Acids Res 33 (suppl 2): W214-W219.
34. DeLano WL, (2002) Pymol: An open-source molecular graphics tool. http://www.pymol.org/.
35. Stuart-harris CH, (1939) A neurotropic strain of human influenza virus. Lancet i: 497-499.
36. Francis TJ, Moore AE, (1940) A study of the neurotropic tendency in strains of the virus of epidemic influenza. J Exp Med 72: 717-728.
37. Gamblin SJ, Haire LF, Russell RJ, Stevens DJ, Xiao B, et al. (2004) The structure and receptor binding properties of the 1918 influenza hemagglutinin. Science 303: 1838-1842.
38. Russell RJ, Haire LF, Stevens DJ, Collins PJ, Lin YP, et al. (2006) The structure of H5N1 avian influenza neuraminidase suggests new opportunities for drug design. Nature 443: 45-49.
39. Varghese JN, Laver WG, Colman PM, (1983) Structure of the influenza virus glycoprotein antigen neuraminidase at 2.9 Å resolution. Nature 303.
40. Colman PM, Varghese JN, Laver WG, (1983) Structure of the catalytic and antigenic sites in influenza virus neuraminidase. Nature 303: 41-44.
41. Garten RJ, Davis CT, Russell CA, Shu B, Lindstrom S, et al. (2009) Antigenic and genetic characteristics of swine-origin 2009 A(H1N1) influenza viruses circulating in humans. Science 325: 197-201.
42. Myers KP, Olsen CW, Gray GC, (2007) Cases of swine influenza in humans: a review of the literature. Clin infect dis 44: 1084-1088.
43. Nelson MI, Viboud C, Simonsen L, Bennett RT, Griesemer SB, et al. (2008) Multiple reassortment events in the evolutionary history of H1N1 influenza A virus since 1918. PLoS Pathog 4: e1000012.
44. Vigerust DJ, Ulett KB, Boyd KL, Madsen J, Hawgood S, et al. (2007) N-linked glycosylation attenuates H3N2 influenza viruses. J Virol 81: 8593-8600.
45. Schwarzer J, Rapp E, Hennig R, Genzel Y, Jordan I, et al. (2009) Glycan analysis in cell culture-based influenza vaccine production: Influence of host cell line and virus strain on the glycosylation pattern of viral hemagglutinin. Vaccine 27: 4325-4336.
46. Lin T, Wang G, Li A, Zhang Q, Wu C, et al. (2009) The hemagglutinin structure of an avian H1N1 influenza A virus. Virology 392: 73-81.
47. Ferguson NM, Cummings DAT, Fraser C, Cajka JC, Cooley PC, et al. (2006) Strategies for mitigating an influenza pandemic. Nature 442: 448-452.
48. Skehel JJ, Wiley DC, (2000) Receptor binding and membrane fusion in virus entry: The Influenza Hemagglutinin. Annu Rev Biochem 69: 531-569.
49. Ha Y, Stevens DJ, Skehel JJ, Wiley DC, (2001) X-ray structures of H5 avian and H9 swine influenza virus hemagglutinins bound to avian and human receptor analogs. Proc Natl Acad Sci U S A 98: 11181-11186.
50. Air GM, Laver WG, Webster RG, Els MC, Luo M, (1989) Antibody recognition of the influenza virus neuraminidase. Cold Spring Harb Symp Quant Biol 54: 247-255.