Exploitation of cytoplasmic and nuclear actin by baculoviruses
TL;DRAbstract
Diverse bacterial and viral pathogens hijack the actin cytoskeleton of host cells to facilitate processes such as attachment, internalization, or spread. Among known pathogens, baculoviruses are unique in their ability to manipulate actin both in the cell cytoplasm and nucleus. We seek to determine how baculoviruses exploit actin to reveal new roles for actin in pathogenesis, and to illuminate the poorly understood function and regulation of nuclear actin. Using time‐lapse microscopy, we find that Autographa californica Multiple Nucleopolyhedrovirus (AcMNPV) undergoes actin‐based motility within the cell cytoplasm. Motility requires p78/83, a viral capsid protein that mimics host WASP proteins and activates actin assembly with the host Arp2/3 complex. As with other pathogens, moving AcMNPV are propelled into surface projections that may function in cell‐to‐cell spread. However, unlike other pathogens, motility also enhances viral collision with the nucleus, enabling translocation into
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Diverse bacterial and viral pathogens hijack the actin cytoskeleton of host cells to facilitate processes such as attachment, internalization, or spread. Among known pathogens, baculoviruses are unique in their ability to manipulate actin both in the cell cytoplasm and nucleus. We seek to determine how baculoviruses exploit actin to reveal new roles for actin in pathogenesis, and to illuminate the poorly understood function and regulation of nuclear actin. Using time‐lapse microscopy, we find that Autographa californica Multiple Nucleopolyhedrovirus (AcMNPV) undergoes actin‐based motility within the cell cytoplasm. Motility requires p78/83, a viral capsid protein that mimics host WASP proteins and activates actin assembly with the host Arp2/3 complex. As with other pathogens, moving AcMNPV are propelled into surface projections that may function in cell‐to‐cell spread. However, unlike other pathogens, motility also enhances viral collision with the nucleus, enabling translocation into
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