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

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

SUBMITTER: Fukushima K 

PROVIDER: S-EPMC5683071 | biostudies-literature | 2015 May

REPOSITORIES: biostudies-literature

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Amino acid substitutions contributing to α2,6-sialic acid linkage binding specificity of human parainfluenza virus type 3 hemagglutinin-neuraminidase.

Fukushima Keijo K   Takahashi Tadanobu T   Ueyama Hiroo H   Takaguchi Masahiro M   Ito Seigo S   Oishi Kenta K   Minami Akira A   Ishitsubo Erika E   Tokiwa Hiroaki H   Takimoto Toru T   Suzuki Takashi T  

FEBS letters 20150411 11

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 linka  ...[more]

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