Amino acid substitutions contributing to alpha 2,6-sialic acid linkage binding specificity of human parainfluenza virus type 3 hemagglutinin-neuraminidase

作者：Fukushima Keijo; Takahashi Tadanobu; Ueyama Hiroo; Takaguchi Masahiro; Ito Seigo; Oishi Kenta; Minami Akira; Ishitsubo Erika; Tokiwa Hiroaki; Takimoto Toru; Suzuki Takashi^*

来源：FEBS LETTERS, 2015, 589(11): 1278-1282.

DOI：10.1016/j.febslet.2015.03.036

• Human parainfluenza virus
• Hemagglutinin-neuraminidase
• Sialyl linkage
• Receptor binding
• Sialic acid
• HN

Human parainfluenza virus type 3 (hPIV3) recognizes both alpha 2,3-and alpha 2,6-linked sialic acids, whereas human parainfluenza virus type 1 (hPIV1) recognizes only alpha 2,3-linked sialic acids. To identify amino acid residues that confer alpha 2,6-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 alpha 2,6-linked sialic acid recognition of the HN3 glycoprotein.

• 出版日期2015-5-8