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