Actin binding and proteolysis by the baculovirus AcMNPV: the role of virion-associated V-CATH.
Infection of larvae by Autographa californica M nuclear polyhedrosis virus (AcMNPV) results in liquefaction of susceptible hosts, presumably due to the breakdown of cells and extracellular matrices. In Spodoptera frugiperda tissue culture cells, infection leads to dramatic rearrangement and eventual destruction of the actin cytoskeleton. The first of these rearrangements is the formation of actin cables in the cytoplasm of the cell. Cable formation requires release of the budded virus (BV) nucleocapsid from the endosome, but does not require new protein synthesis, suggesting that the nucleocapsid contains the activity necessary to induce cable formation. We have identified two distinct BV-associated actin-targeting activities. The first, a nucleocapsid-associated actin-binding activity, enabled actin copelleting and may also induce actin polymerization and cable formation. The second activity, associated with the nucleocapsid and envelope fractions of BV, was a protease that specifically degraded actin. This protease was identified as V-CATH, a cathepsin L-like protease that is a product of the AcMNPV v-cath gene.
Lanier
L M
LM
Department of Molecular and Cell Biology, University of California, Berkeley, 94720, USA.
Slack
J M
JM
Volkman
L E
LE
D000199:Actins / Q000187:drug effects / Q000378:metabolism*; D000818:Animals; D002403:Cathepsins / Q000378:metabolism*; D002460:Cell Line; D015853:Cysteine Proteinase Inhibitors / Q000494:pharmacology; D006868:Hydrolysis; D017924:Nucleopolyhedroviruses / Q000201:enzymology*; D018411:Spodoptera / Q000166:cytology; D014771:Virion / Q000378:metabolism
D000199:Actins; D015853:Cysteine Proteinase Inhibitors; D002403:Cathepsins