Sialidase Activity of Influenza A Virus in an Endocytic Pathway Enhances Viral Replication

Suzuki, Takashi; Takahashi, Toshifumi; Guo, Can; Hidari, Kazuya I.P.J.; Miyamoto, Daisei; Goto, Hideo; Kawaoka, Yoshihiro; Suzuki, Yasuo

doi:10.1128/jvi.79.18.11705-11715.2005

Cited by 92 publications

(74 citation statements)

References 35 publications

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“…30) Recently, sialidase activity of influenza virus sialidase has been reported to function not only in the late stage but also in the initial stage of virus infection cycles, indicating that viral sialidase activity in late endosome/lysosome traffic on cell entry facilitates production of infectious progeny viruses from the infected cells. 31) The results indicate that GH has effects not only in the late stage of IAV infection, such as the assembly and budding of progeny viruses, but also in the early stage, such as virus entry process via the endocytic pathway.…”

Section: Resultsmentioning

confidence: 88%

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Glucosyl Hesperidin Prevents Influenza A Virus Replication <i>in Vitro</i> by Inhibition of Viral Sialidase

Saha

Takahashi

Suzuki

2009

Biological & Pharmaceutical Bulletin

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Hesperidin, a flavonoid obtained from citrus fruits, is known to have multiple biological activities and antimicrobial activities for human viruses; however, hesperidin has very low solubility in water and the target molecule of hesperidin for influenza virus remains unknown. A water-soluble derivative of hesperidin, glucosyl hesperidin (GH), which was synthesized by regioselective transglycosylation with cyclodextrin glucanotransferase, has been reported to have biological activities that are as or stronger than those of hesperidin. To determine the inhibitory effect of GH on influenza A virus (IAV) infection, Madin-Darby canine kidney (MDCK) cells were treated with GH before, at the same time as, and after IAV inoculation. GH treatment before IAV inoculation had no effect on virus replication, whereas, treatment with GH at the same time as or after IAV inoculation induced distinct reduction in IAV replication. Inhibition analysis of GH against two surface glycoprotein spikes of IAV revealed that GH prevents IAV replication by inhibition of viral sialidase activity that is involved in the entry and release stages on IAV infection but not by receptor binding inhibition. GH had no cytotoxic effects on MDCK cells in a dose range of 0-25 mM. Our results provide useful information for the development of novel sialidase inhibitors for influenza prevention.

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Section: Resultsmentioning

confidence: 88%

“…32,33) The low-pH stability of IAV sialidase is functionally linked to virus entry via the endocytic pathway and contributes to the ability of virus replication. 31) The difference of GH effects between A/Aichi/2/68 (H3N2) and other strains may depend on the low-pH stability of their sialidase activities.…”

Section: Resultsmentioning

confidence: 99%

Glucosyl Hesperidin Prevents Influenza A Virus Replication <i>in Vitro</i> by Inhibition of Viral Sialidase

Saha

Takahashi

Suzuki

2009

Biological & Pharmaceutical Bulletin

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“…The sialidase activity has been suggested to be involved in enhancement of virus infection and replication at the early stage of the virus lifecycle such as virus attachment to the host cellular surface and cell entry process, but the mechanism remains unknown. [4][5][6][7] We have found that influenza A virus also showed strong binding to a non-sialo glycoconjugate, sulfatide 8) (Fig. 1).…”

Section: Introductionmentioning

confidence: 84%

Role of Sulfatide in Influenza A Virus Replication

Takahashi

Suzuki

2015

Biological & Pharmaceutical Bulletin

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“…The low-pH stability of NA conferred by 344R and 466F was reported to increase the replication ability of a virus in the MDCK cell line [38]. KBNP-0028 possessed the amino acids associated with the low pH stability, and the high productivity may be attributed to the low pH stability, in part.…”

Section: Discussionmentioning

confidence: 99%

Characterization of a Chicken Embryo-Adapted H9N2 Subtype Avian Influenza Virus

Kwon¹,

Cho²,

Ahn³

et al. 2009

TOVSJ

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Abstract:The low pathogenic avian influenza (LPAI) caused by H9N2 virus has generated economic losses in the Korean poultry industry since 1999, but field isolates could not be used for killed oil emulsion vaccine directly because of low productivity in embryonated chicken eggs (ECE). Therefore, we established a vaccine strain, KBNP-0028, by passage through ECE with allantoic fluid showing the highest volume and titer. KBNP-0028 possessed 158 N-glycan on hemagglutinin (HA) as its parent strain, but acquired a 16 amino acid deletion in the stalk region of neuraminidase (16-del NA) as a result of balancing with the glycosylated HA. KBNP-0028 was sufficiently productive in ECE to be compared with the A/Puerto Rico/8/34 (PR8) strain and immunogenic enough to induce high antibody titers. The antibodies inhibited hemagglutination of recent field isolates as highly as they inhibited KBNP-0028. Genome analysis revealed that KBNP-0028 carried no known mutation relevant to virulence in mammalian. In conclusion, KBNP-0028 is a promising vaccine candidate for prevention of the LPAI in the Republic of Korea.

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Sialidase Activity of Influenza A Virus in an Endocytic Pathway Enhances Viral Replication

Cited by 92 publications

References 35 publications

Glucosyl Hesperidin Prevents Influenza A Virus Replication <i>in Vitro</i> by Inhibition of Viral Sialidase

Glucosyl Hesperidin Prevents Influenza A Virus Replication <i>in Vitro</i> by Inhibition of Viral Sialidase

Role of Sulfatide in Influenza A Virus Replication

Characterization of a Chicken Embryo-Adapted H9N2 Subtype Avian Influenza Virus

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