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A Recombinant Sialidase Fusion Protein Effectively Inhibits Human Parainfluenza Viral Infection In Vitro and In Vivo
Author(s) -
Anne Moscona,
Matteo Porotto,
Samantha G. Palmer,
Caroline G. Tai,
L. M. Aschenbrenner,
Gallen TrianaBaltzer,
QiXiang Li,
David F. Wurtman,
Stefan Niewiesk,
Fang Fang
Publication year - 2010
Publication title -
the journal of infectious diseases
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.69
H-Index - 252
eISSN - 1537-6613
pISSN - 0022-1899
DOI - 10.1086/653621
Subject(s) - sialic acid , sialidase , receptor , in vivo , biology , in vitro , microbiology and biotechnology , virology , glycoprotein , respiratory epithelium , virus , neuraminidase , epithelium , biochemistry , genetics
The first step in infection by human parainfluenza viruses (HPIVs) is binding to the surface of respiratory epithelial cells via interaction between viral receptor-binding molecules and sialic acid-containing receptors. DAS181, a recombinant sialidase protein containing the catalytic domain of Actinomyces viscosus sialidase, removes cell surface sialic acid, and we proposed that it would inhibit HPIV infection.

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