Ontology highlight
ABSTRACT:
SUBMITTER: Bookwalter CS
PROVIDER: S-EPMC5702669 | biostudies-literature | 2017 Nov
REPOSITORIES: biostudies-literature
The Journal of biological chemistry 20171004 47
Motility of the apicomplexan malaria parasite <i>Plasmodium falciparum</i> is enabled by a multiprotein glideosome complex, whose core is the class XIV myosin motor, PfMyoA, and a divergent <i>Plasmodium</i> actin (PfAct1). Parasite motility is necessary for host-cell invasion and virulence, but studying its molecular basis has been hampered by unavailability of sufficient amounts of PfMyoA. Here, we expressed milligram quantities of functional full-length PfMyoA with the baculovirus/<i>Sf</i>9 ...[more]