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.
Accelerating Research
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom
Address
John Eccles HouseRobert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom