v5.1.0.3
Cicer data from the Legume Information System
| Type | Family |
| Description | Bacterial type IV secretion systems mediate the transfer of macromolecular substrates into various target cells, including the transfer of virulence proteins into eukaryotic host cells. The virB operon constitutes a major determinant of virulence [ ]. It mediates invasion, proinflammatory activation and antiapoptotic protection of endothelial cells. VirB-dependent changes of human endothelial cell (HEC) function include massive cytoskeletal rearrangements, a proinflammatory activation by nuclear factor NF-kappa-B, inhibition of early and late events of apoptosis, leading to an increased cell survival, and, at high infection doses, a cytostatic or cytotoxic effect, which interferes with a potent VirB-independent mitogenic activity [, ]. Protein PtlE is a component of the type IV secretion system ptl required for secretion of assembled pertussis toxin (a toxin from Bordetella pertussis) through the outer membrane [ , , ]. PtlE has peptidoglycanase activity and is responsible for the local removal or rearrangement of the peptidoglycan layer during the assembly of the Ptl secretion complex []. |
| Short Name | VirB8/PtlE |