DOI QR코드

DOI QR Code

Development and Characterization of Monoclonal Antibodies against Nucleoprotein for Diagnosis of Influenza A Virus

  • Nguyen, Hong Phuong (Infectious Disease Research Center, Korea Research Institute of Bioscience and Biotechnology) ;
  • Kwak, Chaewon (Infectious Disease Research Center, Korea Research Institute of Bioscience and Biotechnology) ;
  • Heo, Chang-Kyu (Rare Disease Research Center, Korea Research Institute of Bioscience and Biotechnology) ;
  • Cho, Eun Wie (Rare Disease Research Center, Korea Research Institute of Bioscience and Biotechnology) ;
  • Yang, Jihyun (Infectious Disease Research Center, Korea Research Institute of Bioscience and Biotechnology) ;
  • Poo, Haryoung (Infectious Disease Research Center, Korea Research Institute of Bioscience and Biotechnology)
  • Received : 2018.02.02
  • Accepted : 2018.03.13
  • Published : 2018.05.28

Abstract

Influenza, which is a highly contagious disease caused by the influenza A virus, continues to be a major health concern worldwide. Although the accurate and early diagnosis of influenza virus infection is important for controlling the spread of this disease and rapidly initiating antiviral therapy, the current influenza diagnostic kits are limited by their low sensitivity. In this study, we developed several new influenza nucleoprotein (NP)-specific monoclonal antibodies (mAbs) and compared their sensitivity and specificity of those with commercially available anti-NP mAbs. Three mAbs, designated M24.11, M34.3, and M34.33, exhibited higher reactivities to recombinant NPs and A/Puerto Rico/8/1934 (H1N1) viral lysates compared with the commercial mAbs, as assessed using enzyme-linked immunosorbent assays. M34.3 and M34.33 showed higher reactivities with A/California/04/09 (pandemic H1N1) and A/Philippines/2/82 (H3N2) viral lysates than the commercial mAbs. In contrast, M24.11 had marked reactivity with H3N2 but not with pandemic H1N1. Immunofluorescent confocal microscopy showed that the three mAbs effectively detected the presence of influenza virus in lung tissues of mice infected with A/Puerto Rico/8/1934. These results indicate that the newly developed M34.3 and M34.33 mAbs could be useful for the development of influenza diagnostics.

Keywords

References

  1. Webster RG, Bean WJ, Gorman OT, Chambers TM, Kawaoka Y. 1992. Evolution and ecology of influenza A viruses. Microbiol. Rev. 56: 152-179.
  2. Cox NJ, Subbarao K. 1999. Influenza. Lancet 354: 1277-1282. https://doi.org/10.1016/S0140-6736(99)01241-6
  3. Neumann G, Noda T, Kawaoka Y. 2009. Emergence and pandemic potential of swine-origin H1N1 influenza virus. Nature 459: 931-939. https://doi.org/10.1038/nature08157
  4. Molinari NA, Ortega-Sanchez IR, Messonnier ML, Thompson WW, Wortley PM, Weintraub E, et al. 2007. The annual impact of seasonal influenza in the US: measuring disease burden and costs. Vaccine 25: 5086-5096. https://doi.org/10.1016/j.vaccine.2007.03.046
  5. Vemula SV, Zhao J, Liu J, Wang X, Biswas S, Hewlett I. 2016. Current approaches for diagnosis of influenza virus infections in humans. Viruses 8: 96. https://doi.org/10.3390/v8040096
  6. Kumar S, Henrickson KJ. 2012. Update on influenza diagnostics: lessons from the novel H1N1 influenza A pandemic. Clin. Microbiol. Rev. 25: 344-361. https://doi.org/10.1128/CMR.05016-11
  7. Uyeki TM. 2003. Influenza diagnosis and treatment in children: a review of studies on clinically useful tests and antiviral treatment for influenza. Pediatr. Infect. Dis. J. 22: 164-177.
  8. Falsey AR, Murata Y, Walsh EE. 2007. Impact of rapid diagnosis on management of adults hospitalized with influenza. Arch. Intern. Med. 167: 354-360. https://doi.org/10.1001/archinte.167.4.ioi60207
  9. Mizuike R, Sasaki T, Baba K, Iwamoto H, Shibai Y, Kosaka M, et al. 2011. Development of two types of rapid diagnostic test kits to detect the hemagglutinin or nucleoprotein of the swine-origin pandemic influenza A virus H1N1. Clin. Vaccine Immunol. 18: 494-499. https://doi.org/10.1128/CVI.00269-10
  10. Yang M, Berhane Y, Salo T, Li M, Hole K, Clavijo A. 2008. Development and application of monoclonal antibodies against avian influenza virus nucleoprotein. J. Virol. Methods 147: 265-274. https://doi.org/10.1016/j.jviromet.2007.09.016
  11. Drexler JF, Helmer A, Kirberg H, Reber U, Panning M, Muller M, et al. 2009. Poor clinical sensitivity of rapid antigen test for influenza A pandemic (H1N1) 2009 virus. Emerg. Infect. Dis. 15: 1662-1664. https://doi.org/10.3201/eid1510.091186
  12. Uyeki TM, Prasad R, Vukotich C, Stebbins S, Rinaldo CR, Ferng YH, et al. 2009. Low sensitivity of rapid diagnostic test for influenza. Clin. Infect. Dis. 48: e89-e92. https://doi.org/10.1086/597828
  13. Linke S, Neubauer K, Dorner MB, Dorner BG, Pauli G, Schweiger B. 2011. Generation and characterisation of monoclonal antibodies against influenza virus A, subtype H5N1. J. Virol. Methods 175: 85-94. https://doi.org/10.1016/j.jviromet.2011.04.025
  14. Wang W, Huang B, Jiang T, Wang X, Qi X, Gao Y, et al. 2012. Robust immunity and heterologous protection against influenza in mice elicited by a novel recombinant NP-M2e fusion protein expressed in E. coli. PLoS One 7: e52488. https://doi.org/10.1371/journal.pone.0052488
  15. Yang J, Shim SM, Nguyen TQ, Kim EH, Kim K, Lim YT, et al. 2017. Poly-gamma-glutamic acid/chitosan nanogel greatly enhances the efficacy and heterosubtypic cross-reactivity of H1N1 pandemic influenza vaccine. Sci. Rep. 7: 44839. https://doi.org/10.1038/srep44839
  16. Heo CK, Woo MK, Yu DY, Lee JY, Yoo JS, Yoo HS, et al. 2010. Identification of autoantibody against fatty acid synthase in hepatocellular carcinoma mouse model and its application to diagnosis of HCC. Int. J. Oncol. 36: 1453-1459.
  17. Shaw ML, Stone KL, Colangelo CM, Gulcicek EE, Palese P. 2008. Cellular proteins in influenza virus particles. PLoS Pathog. 4: e1000085. https://doi.org/10.1371/journal.ppat.1000085
  18. Heyward JT, Klimas RA, Stapp MD, Obijeski JF. 1977. The rapid concentration and purification of influenza virus from allantoic fluid. Arch. Virol. 55: 107-119. https://doi.org/10.1007/BF01314484
  19. Polson A, Keen A, Sinclair-Smith C, Furminger IG. 1972. Polyethylene glycol purification of influenza virus with respect to aggregation and antigenicity. J. Hyg. (Lond.) 70: 255-265. https://doi.org/10.1017/S0022172400022312
  20. Shu LL, Bean WJ, Webster RG. 1993. Analysis of the evolution and variation of the human influenza A virus nucleoprotein gene from 1933 to 1990. J. Virol. 67: 2723-2729.
  21. Reid AH, Fanning TG, Janczewski TA, Lourens RM, Taubenberger JK. 2004. Novel origin of the 1918 pandemic influenza virus nucleoprotein gene. J. Virol. 78: 12462-12470. https://doi.org/10.1128/JVI.78.22.12462-12470.2004
  22. Babar MM, Zaidi NU. 2015. Protein sequence conservation and stable molecular evolution reveals influenza virus nucleoprotein as a universal druggable target. Infect. Genet. Evol. 34: 200-210. https://doi.org/10.1016/j.meegid.2015.06.030
  23. Ye Q, Krug RM, Tao YJ. 2006. The mechanism by which influenza A virus nucleoprotein forms oligomers and binds RNA. Nature 444: 1078-1082. https://doi.org/10.1038/nature05379
  24. Werthen M, Nygren H. 1988. Effect of antibody affinity on the isotherm of antibody binding to surface-immobilized antigen. J. Immunol. Methods 115: 71-78. https://doi.org/10.1016/0022-1759(88)90311-0

Cited by

  1. Modular Protein Engineering Approach to the Functionalization of Gold Nanoparticles for Use in Clinical Diagnostics vol.1, pp.7, 2018, https://doi.org/10.1021/acsanm.8b00737
  2. Zika Virus Proteins NS2A and NS4A Are Major Antagonists that Reduce IFN-β Promoter Activity Induced by the MDA5/RIG-I Signaling Pathway vol.29, pp.10, 2019, https://doi.org/10.4014/jmb.1909.09017
  3. Novel protein microarray for the detection of avian influenza virus antibodies and simultaneous distinction of antibodies against H5 and H7 subtypes vol.48, pp.6, 2018, https://doi.org/10.1080/03079457.2019.1634791