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Please use this identifier to cite or link to this item: http://repository.li.mahidol.ac.th/dspace/handle/123456789/1657
Title: Substrate specificity of avian influenza H5N1 neuraminidase
Authors: Naruthai Onsirisakul
Nakakita, Shin-ichi
Chompunuch Boonarkart
Alita Kongchanagul
Ornpreya Suptawiwat
Pilaipan Puthavathana
Krisada Chaichuen
Kanokwan Kittiniyom
Suzuki, Yasuo
Prasert Auewarakul
Mahidol University. Faculty of Medical Technology. Department of Clinical Microbiology and Applied Technology
Mahidol University. Faculty of Veterinary Science
Mahidol Univeristy. Faculty of Medicine Siriraj Hospital. Department of Microbiology.
Mahidol University. Institute of Molecular Biosciences
Keywords: H5N1 avian influenza virus;Neuraminidase;Sialic acid;adaptation;substrate preference;Open Access article
Issue Date: 12-Nov-2014
Citation: World Journal of Virology. Vol.3, No.4 (Nov 2014), 30-36
Abstract: AIM: To characterise neuraminidase (NA) substrate specificity of avian influenza H5N1 strains from humans and birds comparing to seasonal influenza virus. METHODS: Avian influenza H5N1 strains from humans and birds were recruited for characterising their NA substrate specificity by using a modified commercial fluorescence Amplex Red assay. This method can identify the preference of α2,6-linked sialic acid or α2,3-linked sialic acid. Moreover, to avoid the bias of input virus, reverse genetic virus using NA gene from human isolated H5N1 were generated and used to compare with the seasonal influenza virus. Lastly, the substrate specificity profile was further confirmed by high-performance liquid chromatography (HPLC) analysis of the enzymatic product. RESULTS: The H5N1 NA showed higher activity on α2,3-linked sialic acid than α2,6-linked (P < 0.0001). To compare the NA activity between the H5N1 and seasonal influenza viruses, reverse genetic viruses carrying the NA of H5N1 viruses and NA from a seasonal H3N2 virus was generated. In these reverse genetic viruses, the NA activity of the H5N1 showed markedly higher activity against α2,3-linked sialic acid than that of the H3N2 virus, whereas the activities on α2,6-linkage were comparable. Interestingly, NA from an H5N1 human isolate that was previously shown to have heamagglutinin (HA) with dual specificity showed reduced activity on α2,3-linkage. To confirm the substrate specificity profile, HPLC analytic of enzymatic product was performed. Similar to Amplex red assay, H5N1 virus showed abundant preference on α2,3-linked sialic acid. CONCLUSION: H5N1 virus maintains the avian specific NA and NA changes may be needed to accompany changes in HA receptor preference for the viral adaptation to humans.
URI: http://repository.li.mahidol.ac.th/dspace/handle/123456789/1657
metadata.dc.identifier.url: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4229813/pdf/WJV-3-30.pdf
ISSN: 2220-3249
Appears in Collections:MT-Article

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