The small 11 kDa nonstructural protein of human parvovirus B19 plays a key role in inducing apoptosis during B19 virus infection of primary erythroid progenitor cells.
Ontology highlight
ABSTRACT: Human parvovirus B19 (B19V) infection shows a strong erythroid tropism and drastically destroys erythroid progenitor cells, thus leading to most of the disease outcomes associated with B19V infection. In this study, we systematically examined the 3 B19V nonstructural proteins, 7.5 kDa, 11 kDa, and NS1, for their function in inducing apoptosis in transfection of primary ex vivo-expanded erythroid progenitor cells, in comparison with apoptosis induced during B19V infection. Our results show that 11 kDa is a more significant inducer of apoptosis than NS1, whereas 7.5 kDa does not induce apoptosis. Furthermore, we determined that caspase-10, an initiator caspase in death receptor signaling, is the most active caspase in apoptotic erythroid progenitors induced by 11 kDa and NS1 as well as durin
SUBMITTER: Chen AY
PROVIDER: S-EPMC2817633 | biostudies-literature | 2010 Feb
REPOSITORIES: biostudies-literature
ACCESS DATA