![]() ![]() One of the virulence proteins, identified as hypersensitive response and pathogenicity factor (HrpF), is a putative translocon of the T3SS. The virulence-associated proteins included T3SS effector proteins and two cell wall degrading enzymes (cellulase and xylosidase). In a medium capable of inducing virulence factor(s), two major proteins, namely, virulence-associated proteins and OM TonB-dependent receptor protein, are secreted. vesicatoria are targeted to OMVs, suggesting that OMVs provide an alternative transport route for T2SS extracellular enzymes ( Sole et al., 2015). campestris, nearly half the proteins that associate with the OMV fraction are involved in virulence, being part of the T3SS, putative virulence factors, or cellulolytic enzymes ( Sidhu et al., 2008).Įlectron microscopy showed that T2SS substrates from X. campestris pv. ![]() In the plant pathogenic bacterium X. campestris pv. The ubiquity of OMVs in the bacterial world suggests that such OMV products may have alternative roles that might modulate bacterial movement and biofilm formation. OMV production may likewise contribute to the movement of other bacteria in porous environments by similarly reducing their contact with environmental constituents. OMV secretion thus is a strategy of X. fastidiosa cells to regulate attachment to surfaces. This process therefore blocks the attachment-driven biofilm formation that would restrict movement of bacteria within the xylem and their colonization of plants. A quorum-sensing system, which suppresses OMV production, serves as an autoinhibitor of bacterial cell adhesion to surfaces. (2014) provided evidence for a novel role for OMVs in Xylella fastidiosa, a bacterial pathogen that colonizes the xylem of important crop plants. Plants, being the major residents on earth, also have to face the bacterial world in their struggle to exist. YashRoy, in Nanostructures for Antimicrobial Therapy, 2017 4.15 OMVs in Plant–Microbe Interactions ![]()
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