Key result
Human metapneumovirus F protein-promoted membrane fusion requires both proteolytic cleavage and exposure to low pH, and occurs independently of the viral G protein.
Population
transiently transfected cells
Design
Preclinical
Authors
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Enables standardized HMPV research in vitro; leaves open questions on clinical translation for infant respiratory disease.
HMPV F protein-promoted fusion requires both proteolytic cleavage by trypsin and exposure to low pH, a mechanism unique among paramyxoviruses.
Schowalter et al. (2006) studied Human metapneumovirus (HMPV) infection (in vitro model). HMPV F protein expression with trypsin and low pH vs. HMPV F protein without trypsin or without low pH was evaluated on Cell-cell membrane fusion (syncytium formation and luciferase reporter activity). Human metapneumovirus F protein-promoted membrane fusion requires both proteolytic cleavage and exposure to low pH, and occurs independently of the viral G protein.