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.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Fukushima K,Takahashi T,Ueyama H,Takaguchi M,Ito S,Oishi K,Minami A,Ishitsubo E,Tokiwa H,Takimoto T,Suzuki T

doi

10.1016/j.febslet.2015.03.036

subject

Has Abstract

pub_date

2015-05-08 00:00:00

pages

1278-82

issue

11

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(15)00238-0

journal_volume

589

pub_type

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