title: Proteinquakes in the evolution of influenza virus hemagglutinin (A/H1N1) under opposing migration and vaccination pressures.
abstract: Influenza virus contains two highly variable envelope glycoproteins, hemagglutinin (HA) and neuraminidase (NA). Here we show that, while HA evolution is much more complex than NA evolution, it still shows abrupt punctuation changes linked to punctuation changes of NA. HA exhibits proteinquakes, which resemble earthquakes and are related to hydropathic shifting of sialic acid binding regions. HA proteinquakes based on shifting sialic acid interactions are required for optimal balance between the receptor-binding and receptor-destroying activities of HA and NA for efficient virus replication. Our comprehensive results present a historical (1945-2011) panorama of HA evolution over thousands of strains and are consistent with many studies of HA and NA interactions based on a few mutations of a few strains.
authors: Department of Physics and Astronomy, Rutgers University, Piscataway, NJ 08854, USA.
authors: J C
authors: JC
authors: Phillips
mesh_terms: D004196:Disease Outbreaks; D019143:Evolution, Molecular; D019267:Hemagglutinin Glycoproteins, Influenza Virus / Q000737:chemistry / Q000235:genetics* / Q000276:immunology; D006801:Humans; D057927:Hydrophobic and Hydrophilic Interactions; D007251:Influenza, Human / Q000453:epidemiology; D009154:Mutation / Q000235:genetics*; D014481:United States / Q000453:epidemiology; D014611:Vaccination
chemical_list: D019267:Hemagglutinin Glycoproteins, Influenza Virus
references: J Mol Biol. 2006 Feb 3;355(5):1143-55
references: 16343533
references: Proc Natl Acad Sci U S A. 1993 Dec 15;90(24):11478-82
references: 8265577
references: Nat Struct Mol Biol. 2008 Jul;15(7):690-8
references: 18596815
references: Proc Natl Acad Sci U S A. 2009 Oct 27;106(43):18137-42
references: 19822741
references: J Exp Med. 2011 Jan 17;208(1):181-93
references: 21220454
references: J Biol Chem. 2011 Feb 4;286(5):3863-72
references: 21118804
references: Protein Eng Des Sel. 2011 Mar;24(3):291-9
references: 21123189
references: Proc Natl Acad Sci U S A. 2011 Aug 23;108(34):13978-83
references: 21825142
references: PLoS One. 2011;6(8):e23374
references: 21886787
references: Proc Natl Acad Sci U S A. 2012 Jan 31;109(5):1494-9
references: 22307603
references: Sci Rep. 2011;1:35
references: 22355554
references: Nat Biotechnol. 2012 Jun;30(6):543-8
references: 22634563
references: Proc Jpn Acad Ser B Phys Biol Sci. 2012;88(6):226-49
references: 22728439
references: Proc Natl Acad Sci U S A. 2012 Aug 21;109(34):13626-31
references: 22869709
references: Int J Mol Sci. 2012;13(7):8398-429
references: 22942711
references: Phys Rev E Stat Nonlin Soft Matter Phys. 2012 Jun;85(6 Pt 2):066121
references: 23005176
references: J Infect Dis. 2013 Jan 1;207(1):98-105
references: 23087428
references: PLoS One. 2013;8(1):e54890
references: 23365683
references: Biomed Res Int. 2014;2014:907381
references: 25143953
references: J Theor Biol. 2001 Sep 7;212(1):57-69
references: 11527445
references: Rev Med Virol. 2002 May-Jun;12(3):159-66
references: 11987141
references: J Am Chem Soc. 2002 Dec 18;124(50):14922-33
references: 12475334
references: J Mol Biol. 1982 May 5;157(1):105-32
references: 7108955
references: Biochemistry. 1992 Oct 13;31(40):9609-21
references: 1327122
references: Phys Rev E Stat Nonlin Soft Matter Phys. 2007 Jan;75(1 Pt 1):011920
references: 17358197