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@ARTICLE{Potapova:642326,
      author       = {Potapova, Anna and Oguchi, Rino and Jimmy, Steffi and
                      Evans, Christopher R. and Yarrington, Kaitlin D. and Winans,
                      James B. and Piepoli, Sofia and Older, Ethan A. and Schakel,
                      Olivia F. and Wetherington, Miles T. and Garvey, William and
                      Floyd, Kyle A. and Vinogradov, Evgeny and Yunker, Peter J.
                      and Sanchez, Laura M. and Nadell, Carey D. and Limoli,
                      Dominique H. and Dietrich, Lars E. P. and Sondermann, Holger
                      and Yildiz, Fitnat H.},
      title        = {{V}ibrio cholerae biofilm matrix assembly and growth are
                      shaped by a glutamate-specific {TAXI}/{TRAP} protein},
      journal      = {Proceedings of the National Academy of Sciences of the
                      United States of America},
      volume       = {122},
      number       = {50},
      issn         = {0027-8424},
      address      = {Washington, DC},
      publisher    = {National Acad. of Sciences},
      reportid     = {PUBDB-2025-05481},
      pages        = {e2504869122},
      year         = {2025},
      abstract     = {Biofilms are critical for the environmental persistence,
                      survival, and infectivity of Vibrio cholerae, the causative
                      agent of cholera. Here, we find that GluP, a
                      glutamate-specific TRAP-TAXI protein, is an uncharacterized
                      matrix component that plays a critical role in biofilm
                      architecture. Loss of GluP reduces biofilm corrugation,
                      expands colony size, and disperses cells from microcolonies,
                      arguing that this factor maintains biofilm structure and
                      organization. While GluP does not affect the abundance or
                      localization of known matrix proteins, its absence reduces
                      Vibrio exopolysaccharide (VPS) production. We determined the
                      crystal structure of GluP, which revealed that GluP binds
                      glutamate, and its biofilm-related phenotypes depend on this
                      binding capability. We further examined the role of GluP in
                      V. cholerae growth under defined conditions where
                      L-glutamate serves as a carbon source, nitrogen source, or
                      both. GluP-deficient strains specifically showed reduced
                      growth when glucose was the carbon source and glutamate the
                      nitrogen source. This defect is dependent on glutamate
                      binding by GluP and highlights its role in coordinating
                      nutrient acquisition and biofilm formation. Importantly,
                      both biofilm assembly and growth defects occurred
                      independently of the predicted membrane component of the Glu
                      TRAP-TAXI system, GluQM. These findings indicate that GluP
                      plays a dual role in biofilm assembly and growth, providing
                      insight into its functional importance in V. cholerae
                      physiology.},
      cin          = {CSSB-DESY-HS},
      ddc          = {500},
      cid          = {I:(DE-H253)CSSB-DESY-HS-20210521},
      pnm          = {633 - Life Sciences – Building Blocks of Life: Structure
                      and Function (POF4-633)},
      pid          = {G:(DE-HGF)POF4-633},
      experiment   = {EXP:(DE-H253)P-P11-20150101},
      typ          = {PUB:(DE-HGF)16},
      doi          = {10.1073/pnas.2504869122},
      url          = {https://bib-pubdb1.desy.de/record/642326},
}