Key result
Inhibition of CTMP-7 or mutation of VP26 decreased HSV-1 viral replication and caused capsid aggregation in the nucleus, demonstrating their interaction is required for viral egress.
The physical interaction between HSV-1 VP26 and host CTMP-7 is crucial for viral capsid enveloping and egress.
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CTMP-7 inhibition curbs HSV-1 replication in animal models; leaves open translation to human antivirals.
HSV-1 viral capsid maturation and egress from the nucleus constitutes a self-controlled process of interactions between host cytoplasmic membrane proteins and viral capsid proteins. In this study, a member of the tetraspanin superfamily, CTMP-7, was shown to physically interact with HSV-1 protein VP26, and the VP26-CTMP-7 complex was detected both in vivo and in vitro. The interaction of VP26 with CTMP-7 plays an essential role in normal HSV-1 replication. Additionally, analysis of a recombinant virus HSV-1-UG showed that mutating VP26 resulted in a decreased viral replication rate and in aggregation of viral mutant capsids in the nucleus. Together, our data support the notion that biological events mediated by a VP26 - CTMP-7 interaction aid in viral capsid enveloping and egress from the cell during the HSV-1 infectious process.
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Wang et al. (2010) studied HSV-1 infection (in vitro). Inhibition of CTMP-7 expression (RNAi) or VP26 mutation vs. Wild-type HSV-1 or control plasmid was evaluated on Viral replication rate and capsid egress. Inhibition of CTMP-7 or mutation of VP26 decreased HSV-1 viral replication and caused capsid aggregation in the nucleus, demonstrating their interaction is required for viral egress.
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