Neuraminidase Amino Acid Sequences of Influenza A/H3N2 and B Viruses Isolated from Influenza Patients in the 2014/15 Japanese Influenza Season

Hideyuki Ikematsu, Yong Jeong, Kenjiro Shirane, Hidehiro Toh, Hiroyuki Sasaki, Shinya Matsumoto, Nozomi Noda, Taeko Hotta, Takeshi Uchiumi, Dongchon Kang

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Abstract

Background: Neuraminidase (NA) is a surface protein essential for influenza virus replication. NA inhibitors are commonly used for the treatment of influenza patients in Japan. Several mutations that reduce the effect of NA inhibitors have been reported. We sequenced the whole NA segment of isolated virus from influenza patients and investigated the relation between the NA amino acid sequence and the 50% inhibitory concentration (IC_50) of four NA inhibitors.

Materials and Methods: Forty A/H3N2 and 19 B influenza virus isolated from patients in the 2014/15 influenza season were analyzed. The IC_50 was determined by a neuraminidase inhibition assay using a fluorescent substrate. Viral RNA was amplified by RT-PCR and the genome was sequenced using a next generation sequencer. The deduced amino acid sequences were analyzed.

Results: There was no AA change in the NA catalytic site of the A/H3N2 and B viruses isolated in the 2014-15 influenza season. There was no significant relation between the NA amino acids and the IC_50 of the four NA inhibitors for A/H3N2 or B viruses.

Conclusion: The catalytic site of NA was highly conserved for these A/H3N2 and B viruses. No emergence of NA amino acid mutations related to the sensitivity of the four currently used NA inhibitors was observed.

Original languageEnglish
Pages (from-to)98-104
Number of pages7
JournalFukuoka igaku zasshi = Hukuoka acta medica
Volume107
Issue number5
Publication statusPublished - May 1 2016

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H3N2 Subtype Influenza A Virus
Influenza B virus
Influenza A virus
Neuraminidase
Human Influenza
Amino Acid Sequence
Cercopithecine Herpesvirus 1
Orthomyxoviridae
Catalytic Domain
Amino Acids
Mutation
Viral RNA
Virus Replication

All Science Journal Classification (ASJC) codes

  • Medicine(all)

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Neuraminidase Amino Acid Sequences of Influenza A/H3N2 and B Viruses Isolated from Influenza Patients in the 2014/15 Japanese Influenza Season. / Ikematsu, Hideyuki; Jeong, Yong; Shirane, Kenjiro; Toh, Hidehiro; Sasaki, Hiroyuki; Matsumoto, Shinya; Noda, Nozomi; Hotta, Taeko; Uchiumi, Takeshi; Kang, Dongchon.

In: Fukuoka igaku zasshi = Hukuoka acta medica, Vol. 107, No. 5, 01.05.2016, p. 98-104.

Research output: Contribution to journalArticle

Ikematsu, Hideyuki ; Jeong, Yong ; Shirane, Kenjiro ; Toh, Hidehiro ; Sasaki, Hiroyuki ; Matsumoto, Shinya ; Noda, Nozomi ; Hotta, Taeko ; Uchiumi, Takeshi ; Kang, Dongchon. / Neuraminidase Amino Acid Sequences of Influenza A/H3N2 and B Viruses Isolated from Influenza Patients in the 2014/15 Japanese Influenza Season. In: Fukuoka igaku zasshi = Hukuoka acta medica. 2016 ; Vol. 107, No. 5. pp. 98-104.
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abstract = "Background: Neuraminidase (NA) is a surface protein essential for influenza virus replication. NA inhibitors are commonly used for the treatment of influenza patients in Japan. Several mutations that reduce the effect of NA inhibitors have been reported. We sequenced the whole NA segment of isolated virus from influenza patients and investigated the relation between the NA amino acid sequence and the 50% inhibitory concentration (IC_50) of four NA inhibitors.Materials and Methods: Forty A/H3N2 and 19 B influenza virus isolated from patients in the 2014/15 influenza season were analyzed. The IC_50 was determined by a neuraminidase inhibition assay using a fluorescent substrate. Viral RNA was amplified by RT-PCR and the genome was sequenced using a next generation sequencer. The deduced amino acid sequences were analyzed.Results: There was no AA change in the NA catalytic site of the A/H3N2 and B viruses isolated in the 2014-15 influenza season. There was no significant relation between the NA amino acids and the IC_50 of the four NA inhibitors for A/H3N2 or B viruses.Conclusion: The catalytic site of NA was highly conserved for these A/H3N2 and B viruses. No emergence of NA amino acid mutations related to the sensitivity of the four currently used NA inhibitors was observed.",
author = "Hideyuki Ikematsu and Yong Jeong and Kenjiro Shirane and Hidehiro Toh and Hiroyuki Sasaki and Shinya Matsumoto and Nozomi Noda and Taeko Hotta and Takeshi Uchiumi and Dongchon Kang",
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T1 - Neuraminidase Amino Acid Sequences of Influenza A/H3N2 and B Viruses Isolated from Influenza Patients in the 2014/15 Japanese Influenza Season

AU - Ikematsu, Hideyuki

AU - Jeong, Yong

AU - Shirane, Kenjiro

AU - Toh, Hidehiro

AU - Sasaki, Hiroyuki

AU - Matsumoto, Shinya

AU - Noda, Nozomi

AU - Hotta, Taeko

AU - Uchiumi, Takeshi

AU - Kang, Dongchon

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N2 - Background: Neuraminidase (NA) is a surface protein essential for influenza virus replication. NA inhibitors are commonly used for the treatment of influenza patients in Japan. Several mutations that reduce the effect of NA inhibitors have been reported. We sequenced the whole NA segment of isolated virus from influenza patients and investigated the relation between the NA amino acid sequence and the 50% inhibitory concentration (IC_50) of four NA inhibitors.Materials and Methods: Forty A/H3N2 and 19 B influenza virus isolated from patients in the 2014/15 influenza season were analyzed. The IC_50 was determined by a neuraminidase inhibition assay using a fluorescent substrate. Viral RNA was amplified by RT-PCR and the genome was sequenced using a next generation sequencer. The deduced amino acid sequences were analyzed.Results: There was no AA change in the NA catalytic site of the A/H3N2 and B viruses isolated in the 2014-15 influenza season. There was no significant relation between the NA amino acids and the IC_50 of the four NA inhibitors for A/H3N2 or B viruses.Conclusion: The catalytic site of NA was highly conserved for these A/H3N2 and B viruses. No emergence of NA amino acid mutations related to the sensitivity of the four currently used NA inhibitors was observed.

AB - Background: Neuraminidase (NA) is a surface protein essential for influenza virus replication. NA inhibitors are commonly used for the treatment of influenza patients in Japan. Several mutations that reduce the effect of NA inhibitors have been reported. We sequenced the whole NA segment of isolated virus from influenza patients and investigated the relation between the NA amino acid sequence and the 50% inhibitory concentration (IC_50) of four NA inhibitors.Materials and Methods: Forty A/H3N2 and 19 B influenza virus isolated from patients in the 2014/15 influenza season were analyzed. The IC_50 was determined by a neuraminidase inhibition assay using a fluorescent substrate. Viral RNA was amplified by RT-PCR and the genome was sequenced using a next generation sequencer. The deduced amino acid sequences were analyzed.Results: There was no AA change in the NA catalytic site of the A/H3N2 and B viruses isolated in the 2014-15 influenza season. There was no significant relation between the NA amino acids and the IC_50 of the four NA inhibitors for A/H3N2 or B viruses.Conclusion: The catalytic site of NA was highly conserved for these A/H3N2 and B viruses. No emergence of NA amino acid mutations related to the sensitivity of the four currently used NA inhibitors was observed.

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