Recombinant sialidase NanA (rNanA) cleaves α2-3 linked sialic acid of host cell surface N-linked glycoprotein to promote Edwardsiella tarda infection》.pdf

Recombinant sialidase NanA (rNanA) cleaves α2-3 linked sialic acid of host cell surface N-linked glycoprotein to promote Edwardsiella tarda infection》.pdf

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Recombinant sialidase NanA (rNanA) cleaves α2-3 linked sialic acid of host cell surface N-linked glycoprotein to promote Edwardsiella tarda infection》.pdf

Fish Shellfish Immunology 47 (2015) 34e45 Contents lists available at ScienceDirect Fish Shellfish Immunology journal homepage: www.elsevier.c om/locate/fsi Full length article Recombinant sialidase NanA (rNanA) cleaves a2-3 linked sialic acid of host cell surface N-linked glycoprotein to promote Edwardsiella tarda infection Petros Kingstone Chigwechokha a, b, Mutsumi Tabata c, Sayaka Shinyoshi c, Kazuki Oishi c, Kyosuke Araki a, c, Masaharu Komatsu a, c, Takao Itakura a, c, Kazuhiro Shiozaki a, c, * a The United Graduate School of Agricultural Sciences, Kagoshima University, Kagoshima, Japan b Department of Fisheries, Mzuzu University, Mzuzu, Malawi c Faculty of Fisheries, Kagoshima University, Kagoshima, Japan a r t i c l e i n f o a b s t r a c t Article history: Edwardsiella tarda is one of the major pathogenic bacteria affecting both marine and freshwater fish Received 30 April 2015 species. Sialidase NanA expressed endogenously in E. tarda is glycosidase removing sialic acids from Received in revised form glycoconjugates. Recently, the relationship of NanA sialidase activity to E. tarda infection has been re- 12 August 2015 ported, however, the mechanism with which sialidase NanA aids the pathogenicity of E. tarda remained Accepted 14 August 2015 unclear. Here, we comprehensively determined the biochemical properties of NanA towards various Available online 17 August 2015

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