Key result
HRV 3A recruits PI4KIIIβ to replication sites independently of GBF1 and ACBD3 unlike other enterovirus proteins.
Why the study?
The mechanisms by which human rhinovirus 3A proteins recruit PI4KIIIβ to replication sites, independent of GBF1 and ACBD3, were unclear.
HRV 3A's distinct mechanism highlights enterovirus diversity; leaves open selective PI4KIIIβ targeting for rhinovirus antivirals.
PI4KIIIβ recruitment to Golgi membranes relies on GBF1/Arf and ACBD3. Enteroviruses such as poliovirus and coxsackievirus recruit PI4KIIIβ to their replication sites via their 3A proteins. Here, we show that human rhinovirus (HRV) 3A also recruited PI4KIIIβ to replication sites. Unlike other enterovirus 3A proteins, HRV 3A failed to bind GBF1. Although HRV 3A was previously shown to interact with ACBD3, our data suggest that PI4KIIIβ recruitment occurred independently of both GBF1 and ACBD3.
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Dorobantu et al. (2014) studied Rhinovirus infection. Human rhinovirus (HRV) 3A protein vs. Other enterovirus 3A proteins was evaluated on PI4KIIIβ recruitment to replication sites. Human rhinovirus (HRV) 3A recruited PI4KIIIβ to replication sites independently of both GBF1 and ACBD3, unlike other enterovirus 3A proteins.
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