IndraLab

Statements


| 3 6

sparser
"We investigated Bap1 binding to OmpT, a major outer membrane porin of V. cholerae containing an integrin-binding domain (LDV peptide)."

sparser
"In presence of PmB, Bap1 was not able to bind to the OmpT protein from the Δ ompT /pBR- ompT * (LDV mutant) mutant to the same extent as to the wild type OmpT protein ( xref ), suggesting a role for the LDV domain in Bap1 binding to OmpT on OMVs ( xref )."

sparser
"Taken together, our results strongly support the hypothesis that Bap1 binds to OmpT on OMVs of V. cholerae A1552 through the LDV tripeptide integrin-binding domain of OmpT."

sparser
"Bap1-OmpT interaction requires the presence of the integrin-binding domain (leucine-aspartic acid-valine LDV peptide) of OmpT and the FG-GAP domains of Bap1 ( xref )."

reach
"It has been reported that Bap1 could associate with outer membrane vesicles (OMVs) by binding to OmpT."

reach
"We investigated Bap1 binding to OmpT, a major outer membrane porin of V. cholerae containing an integrin binding domain (LDV peptide)."

reach
"Taken together, our results strongly support the hypothesis that Bap1 binds to OmpT on OMVs of V. cholerae A1552 through the LDV tripeptide integrin binding domain of OmpT."

sparser
"It was also reported that RbmC does not interact with OmpT in the OMVs, although it is currently unclear why Bap1, but not RbmC, binds to OmpT."

sparser
"Under polymyxin B-induced stress conditions, Vibrio cholerae O1 El Tor produces BMVs containing the protein OmpT that binds the secreted protein Bap1, which in turn binds the AMP LL-37 ( xref )."