title: Preliminary crystallographic analysis of neuraminidase N2 from a new influenza A virus.
abstract: Influenza virus is a major viral respiratory pathogen that causes yearly epidemics in temperate climates. The H3N2 subtype is one of the major causative agents of severe epidemics and plays a critical role in vaccine development. The neuraminidase (NA) inhibitors oseltamivir and zanamivir are two commercially available NA-targeted competitive antiviral drugs. However, their effectiveness has been compromised by the rapid emergence of resistance. Q136K is a novel mutation in NA which confers resistance to zanamivir. In this study, a Q136K mutant N2 protein was expressed in a baculovirus system and crystals were obtained. The crystal of N2 belonged to space group P2₁2₁2₁, with unit-cell parameters a = 109.5, b = 112.8, c = 165.2 Å. Data were collected to 2.4 Å resolution. Four monomers were found in the asymmetric unit. The Matthews coefficient and solvent content were calculated to be 3.0 Å³ Da⁻¹ and 59.0%, respectively.
authors.affiliation: School of Life Sciences, Sichuan University, Chengdu 610064, People's Republic of China.
authors.forename: Feng
authors.initials: F
authors.lastname: Gao
authors.forename: Jinku
authors.initials: J
authors.lastname: Bao
mesh_terms: D018360:Crystallography, X-Ray; D015967:Gene Expression Regulation, Viral; D006801:Humans; D053122:Influenza A Virus, H3N2 Subtype / Q000201:enzymology* / Q000235:genetics; D009154:Mutation / Q000235:genetics; D009439:Neuraminidase / Q000737:chemistry* / Q000235:genetics
chemical_list: C403285:NEU2 protein, human; D009439:Neuraminidase
keywords: drug resistance; influenza A virus; neuraminidases
references.citation: Acta Crystallogr D Biol Crystallogr. 2011 Apr;67(Pt 4):355-67
references.pmid: 21460454
references.citation: Arch Virol. 2013 Apr;158(4):859-76
references.pmid: 23435952
references.citation: Nat Commun. 2010 Nov 16;1:113
references.pmid: 21081911
references.citation: Acta Crystallogr D Biol Crystallogr. 2010 Jan;66(Pt 1):22-5
references.pmid: 20057045
references.citation: J Virol. 2009 Oct;83(20):10366-73
references.pmid: 19641000
references.citation: Annu Rev Biochem. 2009;78:95-118
references.pmid: 19254207
references.citation: Sci Rep. 2013;3:1551
references.pmid: 23531861
references.citation: Emerg Infect Dis. 2009 Dec;15(12):1970-2
references.pmid: 19961677
references.citation: Methods Enzymol. 1997;276:307-26
references.pmid: 27754618
references.citation: Nat Struct Mol Biol. 2010 Oct;17(10):1266-8
references.pmid: 20852645
references.citation: Emerg Infect Dis. 2011 Feb;17(2):283-6
references.pmid: 21291607
references.citation: J Mol Biol. 1993 Aug 20;232(4):1069-83
references.pmid: 8371267
references.citation: J Virol. 2008 Nov;82(21):10493-501
references.pmid: 18715929
references.citation: Nature. 2006 Sep 7;443(7107):45-9
references.pmid: 16915235
references.citation: J Gen Virol. 2013 Feb;94(Pt 2):293-297
references.pmid: 23329681
references.citation: J Mol Biol. 1968 Apr 28;33(2):491-7
references.pmid: 5700707
references.citation: J Mol Biol. 1991 Sep 20;221(2):473-86
references.pmid: 1920428
references.citation: Nature. 2005 Oct 20;437(7062):1108
references.pmid: 16228009