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Increased Pathogenicity of West Nile Virus (WNV) by Glycosylation of Envelope Protein and Seroprevalence of WNV in Wild Birds in Far Eastern Russia

Author

Listed:
  • Hiroaki Kariwa

    (Laboratory of Public Health, Department of Environmental Veterinary Sciences, Graduate School of Veterinary Medicine, Hokkaido University, Kita-18, Nishi-9, Kita-Ku, Sapporo 060-0818, Japan)

  • Ryo Murata

    (Laboratory of Public Health, Department of Environmental Veterinary Sciences, Graduate School of Veterinary Medicine, Hokkaido University, Kita-18, Nishi-9, Kita-Ku, Sapporo 060-0818, Japan
    Laboratory of Animal Health, Department of Animal Science, Faculty of Agriculture, Tokyo University of Agriculture, Funako 1737, Atsugi 243-0034, Japan)

  • Masashi Totani

    (Laboratory of Public Health, Department of Environmental Veterinary Sciences, Graduate School of Veterinary Medicine, Hokkaido University, Kita-18, Nishi-9, Kita-Ku, Sapporo 060-0818, Japan
    Third Animal Quarantine Division, Animal Quarantine Service, Narita Branch, Ministry of Agriculture, Forestry and Fisheries, Ohaza Tennami, Sanrizuka, Aza Nishihara 254-1, Narita 282-0011, Japan)

  • Kentaro Yoshii

    (Laboratory of Public Health, Department of Environmental Veterinary Sciences, Graduate School of Veterinary Medicine, Hokkaido University, Kita-18, Nishi-9, Kita-Ku, Sapporo 060-0818, Japan)

  • Ikuo Takashima

    (Laboratory of Public Health, Department of Environmental Veterinary Sciences, Graduate School of Veterinary Medicine, Hokkaido University, Kita-18, Nishi-9, Kita-Ku, Sapporo 060-0818, Japan
    Department of Nutrition, Faculty of Nursing and Nutrition, Tenshi College, Kita-13, Higashi-3-1-30, Higashi-Ku, Sapporo 065-0013, Japan)

Abstract

In this review, we discuss the possibility that the glycosylation of West Nile (WN) virus E-protein may be associated with enhanced pathogenicity and higher replication of WN virus. The results indicate that E-protein glycosylation allows the virus to multiply in a heat-stable manner and therefore, has a critical role in enhanced viremic levels and virulence of WN virus in young-chick infection model. The effect of the glycosylation of the E protein on the pathogenicity of WN virus in young chicks was further investigated. The results indicate that glycosylation of the WN virus E protein is important for viral multiplication in peripheral organs and that it is associated with the strong pathogenicity of WN virus in birds. The micro-focus reduction neutralization test (FRNT) in which a large number of serum samples can be handled at once with a small volume (15 μL) of serum was useful for differential diagnosis between Japanese encephalitis and WN virus infections in infected chicks. Serological investigation was performed among wild birds in the Far Eastern region of Russia using the FRNT. Antibodies specific to WN virus were detected in 21 samples of resident and migratory birds out of 145 wild bird samples in the region.

Suggested Citation

  • Hiroaki Kariwa & Ryo Murata & Masashi Totani & Kentaro Yoshii & Ikuo Takashima, 2013. "Increased Pathogenicity of West Nile Virus (WNV) by Glycosylation of Envelope Protein and Seroprevalence of WNV in Wild Birds in Far Eastern Russia," IJERPH, MDPI, vol. 10(12), pages 1-21, December.
  • Handle: RePEc:gam:jijerp:v:10:y:2013:i:12:p:7144-7164:d:31256
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