Mutations at the monomer-monomer interface away from the active site of influenza B virus neuraminidase reduces susceptibility to neuraminidase inhibitor drugs

Journal of Infection and Chemotherapy

Volumn 19, Issue 5, 2013, Pages 891-895

  Fujisaki, Seiichiro ^a   Imai, Masaki ^a   Takashita, Emi ^a   Taniwaki, Tae ^b   Xu, Hong ^a   Kishida, Noriko ^a   Yokoyama, Masaru ^a   Sato, Hironori ^a   Tashiro, Masato ^a   Odagiri, Takato ^a  

^a NATIONAL INSTITUTE OF INFECTIOUS DISEASES   (Japan)

^b Kochi Public Health and Sanitation Institute   (Japan)

Author keywords

Influenza B virus; Neuraminidase protein; Neuraminidase inhibitor resistant; Novel substitutions in

Indexed keywords

4 ACETAMIDO 5 AMINO 3 (1 ETHYLPROPOXY) 1 CYCLOHEXENE 1 CARBOXYLIC ACID; LANINAMIVIR; PERAMIVIR; SIALIDASE INHIBITOR; VIRUS SIALIDASE; ZANAMIVIR;

AMINO ACID SUBSTITUTION; ANIMAL CELL; ANTIVIRAL SUSCEPTIBILITY; ANTIVIRAL THERAPY; ARTICLE; CHILD; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME ASSAY; ENZYME INHIBITION; ENZYME STRUCTURE; G140R GENE; GENE MUTATION; GENETIC ASSOCIATION; GENETIC SELECTION; HUMAN; INFANT; INFLUENZA VIRUS B; INOCULATION; MALE; MDCK CELL; NONHUMAN; P139S GENE; PRESCHOOL CHILD; PYROSEQUENCING; Q138R GENE; SCHOOL CHILD; SEQUENCE ANALYSIS; VIRUS GENE; VIRUS ISOLATION; VIRUS MUTATION;

ANIMALS; ANTIVIRAL AGENTS; CATALYTIC DOMAIN; DOGS; DRUG RESISTANCE, VIRAL; ENZYME INHIBITORS; HUMANS; INFLUENZA B VIRUS; INFLUENZA, HUMAN; JAPAN; MADIN DARBY CANINE KIDNEY CELLS; MODELS, MOLECULAR; MUTATION; NEURAMINIDASE; OSELTAMIVIR; VIRAL PROTEINS; ZANAMIVIR;

EID: 84885952463     PISSN: 1341321X     EISSN: 14377780     Source Type: Journal    
DOI: 10.1007/s10156-013-0589-6     Document Type: Article

References (20)

1. Palese P, Tobita K, Ueda M, Compans RW. Characterization of temperature-sensitive influenza virus mutants defective in neuraminidase. Virology. 1974;61:397-410.
2. Liu C, Eichelberger MC, Compans RW, Air GM. Influenza type A virus neuraminidase does not play a role in viral entry, replication, assembly, or budding. J Virol. 1995;69:1099-106.
3. Bossart-Whitaker P, Carson M, Babu YS, Smith CD, Laver WG, Air GM. Three-dimensional structure of influenza A N9 neuraminidase and its complex with the inhibitor 2-deoxy 2,3-dehydro-N-acetyl neuraminic acid. J Mol Biol. 1993;232:1069-83.
4. Varghese JN, McKimm-Breschkin JL, Caldwell JB, Kortt AA, Colman PM. The structure of the complex between influenza virus neuraminidase and sialic acid, the viral receptor. Proteins. 1992;14:327-32.
5. Varghese JN, Epa VC, Colman PM. Three-dimensional structure of the complex of 4-guanidino-Neu5Ac2en and influenza virus neuraminidase. Protein Sci. 1995;4:1081-7.
6. Burmeister WP, Ruigrok RW, Cusack S. The 2.2-Å resolution crystal structure of influenza B neuraminidase and its complex with sialic acid. EMBO J. 1992;11:49-56.
7. Oakley AJ, Barrett S, Peat TS, Newman J, Streltsov VA, Waddington L, et al. Structural and functional basis of resistance to neuraminidase inhibitors of influenza B viruses. J Med Chem. 2010;53:6421-31.
8. Fujisaki S, Takashita E, Yokoyama M, Taniwaki T, Xu H, Kishida N, et al. A single E105K mutation far from the active site of influenza B virus neuraminidase contributes to reduced susceptibility to multiple neuraminidase-inhibitor drugs. Biochem Biophys Res Commun. 2012;429:51-6.
9. Bastien N, Gubbay JB, Richardson D, Sleeman K, Gubareva L, Li Y. Detection of an influenza B virus strain with reduced susceptibility to neuraminidase inhibitor drugs. J Clin Microbiol. 2011;49:4020-1.
10. Hurt AC, Iannello P, Jachno K, Komadina N, Hampson AW, Barr IG, et al. Neuraminidase inhibitor-resistant and -sensitive influenza B viruses isolated from an untreated human patient. Antimicrob Agents Chemother. 2006;50:1872-4.
11. Ujike M, Ejima M, Anraku A, Shimabukuro K, Obuchi M, Kishida N, et al. Monitoring and characterization of oseltamivir-resistant pandemic (H1N1) 2009 virus, Japan, 2009-2010. Emerg Infect Dis. 2011;17:470-9.
12. Meetings of the WHO working group on surveillance of influenza antiviral susceptibility: Geneva, November 2011 and June 2012. Weekly Epidemiological Record/Health Section of the Secretariat of the League of Nations. 2012;87:369-374.
13. Okomo-Adhiambo M, Nguyen HT, Sleeman K, Sheu TG, Deyde VM, Garten RJ, et al. Host cell selection of influenza neuraminidase variants: implications for drug resistance monitoring in A(H1N1) viruses. Antiviral Res. 2010;85:381-8.
14. Hurt AC, Holien JK, Parker M, Kelso A, Barr IG. Zanamivir-resistant influenza viruses with a novel neuraminidase mutation. J Virol. 2009;83:10366-73.
15. Yen H-L, Hoffmann E, Taylor G, Scholtissek C, Monto AS, Webster RG, et al. Importance of neuraminidase active-site residues to the neuraminidase inhibitor resistance of influenza viruses. J Virol. 2006;80:8787-95.
16. Hatakeyama S, Sugaya N, Ito M, Yamazaki M, Ichikawa M, Kimura K, et al. Emergence of influenza B viruses with reduced sensitivity to neuraminidase inhibitors. JAMA. 2007;297:1435-42.
17. Carr S, Ilyushina NA, Franks J, Adderson EE, Caniza M, Govorkova EA, et al. Oseltamivir-resistant influenza A and B viruses pre- and postantiviral therapy in children and young adults with cancer. Pediatr Infect Dis J. 2011;30:284-8.
18. Colman PM, Hoyne PA, Lawrence MC. Sequence and structure alignment of paramyxovirus hemagglutinin-neuraminidase with influenza virus neuraminidase. J Virol. 1993;67:2972-80.
19. Garg S, Moore Z, Lee N, McKenna J, Bishop A, Fleischauer A, et al. A Cluster of patients infected with I221V influenza B virus variants with reduced oseltamivir susceptibility: North Carolina and South Carolina, 2010-2011. J Infect Dis 2012. doi: 10.1093/infdis/jis776.
20. Collins PJ, Haire LF, Lin YP, Liu J, Russell RJ, Walker PA, et al. Crystal structures of oseltamivir-resistant influenza virus neuraminidase mutants. Nature (Lond). 2008;453:1258-61.