Key result
Trypsinized double-shelled rotavirus virions induced fluorophore release from membrane vesicles, indicating that membrane destabilization by outer capsid proteins leads to permeabilization.
Membrane destabilization caused by trypsinized outer capsid proteins of rotavirus leads to fluorophore release, suggesting a mechanism for viral entry into host cells.
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Hypothesis-generating for rotavirus entry; leaves open translation to human pathogenesis or antiviral targets.
Ruíz et al. (1994) studied Rotavirus infection mechanism. Trypsinized double-shelled rotavirus virions vs. Purified single-shelled particles and untrypsinized double-shelled ones was evaluated on Fluorophore release (dequenching) from membrane vesicles. Trypsinized double-shelled rotavirus virions induced fluorophore release from membrane vesicles, indicating that membrane destabilization by outer capsid proteins leads to permeabilization.
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