A classical anti-autophagic viral protein reshapes mitochondria for immune evasion

一种经典的抗自噬病毒蛋白重塑线粒体以逃避免疫攻击

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Abstract

Viral subversion of macroautophagy/autophagy is a well-established immune evasion strategy, with BCL2 homologs from γ-herpesviruses serving as prototypical inhibitors through BECN1 (beclin 1) sequestration. Yet the full spectrum of their functions remains incompletely understood. In our recent study, we uncovered a non-canonical role for the Kaposi's sarcoma-associated herpesvirus (KSHV)-encoded BCL2 homolog (vBCL2) during late lytic replication. Unexpectedly, vBCL2 hijacks the host NDP kinase NME2/NM23-H2 to activate the mitochondrial fission GTPase DNM1L/DRP1, promoting mitochondrial fragmentation. This organelle remodeling dismantles MAVS-mediated antiviral signaling and facilitates virion assembly. A vBCL2 mutant unable to bind NME2 fails to induce fission or complete the viral lifecycle. These findings provide a long-sought answer to why vBCL2 is indispensable during lytic infection, and uncover a new immune evasion strategy centered on mitochondrial control. Our work expands the current view of virus-organelle interactions beyond canonical autophagy control and offers new targets for therapeutic intervention.

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