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Literature summary for 3.2.1.18 extracted from

  • Alymova, I.V.; Taylor, G.; Mishin, V.P.; Watanabe, M.; Murti, K.G.; Boyd, K.; Chand, P.; Babu, Y.S.; Portner, A.
    Loss of the N-linked glycan at residue 173 of human parainfluenza virus type 1 hemagglutinin-neuraminidase exposes a second receptor-binding site (2008), J. Virol., 82, 8400-8410.
    View publication on PubMedView publication on EuropePMC

Protein Variants

Protein Variants Comment Organism
N173S mutant sensitive to 4-azido-5-isobutyrylamino-2,3-didehydro-2,3,4,5-tetradeoxy-d-glycero-d-galacto-2-nonulopyranosic acid in neuraminidase inhibition assays but more than 10000fold less sensitive to the compound in hemagglutination inhibition tests than a recombinant Sendai virus whose hemagglutinin-neuraminidase is replaced with that of human parainfluenza virus-1. Its susceptibility to 4-azido-5-isobutyrylamino-2,3-didehydro-2,3,4,5-tetradeoxy-d-glycero-d-galacto-2-nonulopyranosic acid in plaque reduction assays is reduced fivefold and does not differ from that of recombinant Sendai virus whose hemagglutinin-neuraminidase was replaced with that of human parainfluenza virus-1 in mice. The N173S mutant fails to be efficiently eluted from erythrocytes and released from cells. It demonstrates reduced growth in cell culture and superior growth in mice. Rresults are consistent with the loss of the N-linked glycan at residue 173 in the mutant. Study suggests that the N-linked glycan at residue 173 masks a second receptor-binding site Human respirovirus 3

Inhibitors

Inhibitors Comment Organism Structure
4-azido-5-isobutyrylamino-2,3-didehydro-2,3,4,5-tetradeoxy-d-glycero-d-galacto-2-nonulopyranosic acid i.e. BCX 2798. Effectively inhibits the activities of the hemagglutinin-neuraminidase of human parainfluenza viruses in vitro and protects mice from lethal infection with a recombinant Sendai virus whose hemagglutinin-neuraminidase was replaced with that of human parainfluenza virus-1 Human respirovirus 3

Organism

Organism UniProt Comment Textmining
Human respirovirus 3
-
types 1 to 3
-

Posttranslational Modification

Posttranslational Modification Comment Organism
glycoprotein the N-linked glycan at residue N173 may mask a second receptor-binding site Human respirovirus 3