Uncoating of human rhinovirus serotype 2 occurs in intact late endosomes at pH 5.5, a process requiring ATP and prevented by the V-ATPase inhibitor bafilomycin A1.
HRV2 uncoating occurs in intact late endosomes at an acidic pH of 5.5, independent of direct receptor involvement.
The internalization pathway and mechanism of uncoating of human rhinovirus serotype 2 (HRV2), a minor-group human rhinovirus, were investigated. Kinetic analysis revealed a late endosomal compartment as the site of capsid modification from D to C antigenicity. The conformational change as well as the infection was prevented by the specific V-ATPase inhibitor bafilomycin A1. A requirement for ATP was also demonstrated with purified endosomes in vitro. Capsid modifications occurred at a pH of 5.5 regardless of whether the virus was entrapped in isolated endosomes or free in solution. These findings suggest that the receptor is not directly involved in the structural modification of HRV2. Viral particles found in purified endosomes of infected cells were mostly devoid of RNA. This supports the hypothesis that uncoating of HRV2 occurs in intact endosomes rather than by a mechanism involving endosomal disruption with subsequent release of the RNA into the cytoplasm.
Prchla et al. (1994) studied Human rhinovirus serotype 2 infection (in vitro). Bafilomycin A1 was evaluated on Capsid modification and uncoating mechanism. Uncoating of human rhinovirus serotype 2 occurs in intact late endosomes at pH 5.5, a process requiring ATP and prevented by the V-ATPase inhibitor bafilomycin A1.
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