IndraLab

Statements


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sparser
"In a subsequent study from the same group, Wong et al. demonstrated that PtpA binds to subunit H of the host vacuolar ATPase (V-ATPase) in the phagosome membrane and that the macrophage class C sorting complex associates with the V-ATPase during phagosome maturation ( xref )."

sparser
"PtpA also binds to subunit H of macrophage V-ATPase and blocks its activity required for phagosome acidification xref ."

sparser
"PtpA binds subunit H of the V-ATPase (Wong et al., xref ) and it also binds to and dephosphorylates VPS33B (Bach et al., xref ), a protein enabling endosome to lysosome trafficking (Galmes et al., xref )."

sparser
"However, the interaction between PtpA and subunit H was found to be through protein-protein interaction, suggesting that V-ATPase is not the catalytic substrate of PtpA ( xref )."

sparser
"PtpA, which binds subunit H of V-ATPase and thereby excludes the proton pump from phagosomes, is a candidate for this missing SecA2-exported effector [ xref ]."

sparser
"Recent study identified that PtpA-mediated exhaustion of host V-ATPase is a two-step process: PtpA interacts with the subunit H of the host V-ATPase machinery initially disrupts the membrane tethering[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

sparser
"Subsequent studies suggested that PtpA also binds to the subunit H of vacuolar-H(+)–ATPase (V-ATPase) machinery (identified by a ‘substrate trapping’ assay), a multisubunit protein complex."

sparser
"Wong et al. ( xref ) demonstrated that PtpA directly binds to the V1 subunit H to: i) block the trafficking of this subunit to the mycobacterial phagosome and ii) block its interaction with Vps33B ( xref )."