title: Amino acid substitutions contributing to α2,6-sialic acid linkage binding specificity of human parainfluenza virus type 3 hemagglutinin-neuraminidase.
abstract: Human parainfluenza virus type 3 (hPIV3) recognizes both α2,3- and α2,6-linked sialic acids, whereas human parainfluenza virus type 1 (hPIV1) recognizes only α2,3-linked sialic acids. To identify amino acid residues that confer α2,6-linked sialic acid recognition of hPIV3, amino acid residues in or neighboring the sialic acid binding pocket of the hPIV3 hemagglutinin-neuraminidase (HN) glycoprotein were substituted for the corresponding residues of hPIV1 HN. Hemadsorption assay with sialyl linkage-modified red blood cells indicated that amino acid residues at positions 275, 277, 372, and 426 contribute to α2,6-linked sialic acid recognition of the HN3 glycoprotein.
authors: Department of Biochemistry, School of Pharmaceutical Sciences, University of Shizuoka, Shizuoka 4228526, Japan.
authors: Keijo
authors: K
authors: Fukushima
authors: Department of Biochemistry, School of Pharmaceutical Sciences, University of Shizuoka, Shizuoka 4228526, Japan.
authors: Tadanobu
authors: T
authors: Takahashi
authors: Department of Biochemistry, School of Pharmaceutical Sciences, University of Shizuoka, Shizuoka 4228526, Japan.
authors: Hiroo
authors: H
authors: Ueyama
authors: Department of Biochemistry, School of Pharmaceutical Sciences, University of Shizuoka, Shizuoka 4228526, Japan.
authors: Masahiro
authors: M
authors: Takaguchi
authors: Department of Biochemistry, School of Pharmaceutical Sciences, University of Shizuoka, Shizuoka 4228526, Japan.
authors: Seigo
authors: S
authors: Ito
authors: Department of Biochemistry, School of Pharmaceutical Sciences, University of Shizuoka, Shizuoka 4228526, Japan.
authors: Kenta
authors: K
authors: Oishi
authors: Department of Biochemistry, School of Pharmaceutical Sciences, University of Shizuoka, Shizuoka 4228526, Japan.
authors: Akira
authors: A
authors: Minami
authors: Department of Chemistry, Faculty of Science, Rikkyo University, Tokyo 1718501, Japan.
authors: Erika
authors: E
authors: Ishitsubo
authors: Department of Chemistry, Faculty of Science, Rikkyo University, Tokyo 1718501, Japan.
authors: Hiroaki
authors: H
authors: Tokiwa
authors: Department of Microbiology and Immunology, University of Rochester Medical Center, Rochester, NY, USA.
authors: Toru
authors: T
authors: Takimoto
authors: Department of Biochemistry, School of Pharmaceutical Sciences, University of Shizuoka, Shizuoka 4228526, Japan. Electronic address: suzukit@u-shizuoka-ken.ac.jp.
authors: Takashi
authors: T
authors: Suzuki
mesh_terms: D019943:Amino Acid Substitution; D000818:Animals; D001665:Binding Sites; D002460:Cell Line; D004912:Erythrocytes / Q000737:chemistry / Q000378:metabolism; D015707:HN Protein / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D000882:Haplorhini; D006801:Humans; D020125:Mutation, Missense; D010224:Parainfluenza Virus 3, Human / Q000201:enzymology* / Q000235:genetics; D012794:Sialic Acids / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D013379:Substrate Specificity / Q000235:genetics
chemical_list: D015707:HN Protein; D012794:Sialic Acids
keywords: HN; Hemagglutinin–neuraminidase; Human parainfluenza virus; Receptor binding; Sialic acid; Sialyl linkage