@article{fdi:010064843,
  title = {{A}lnus peptides modify membrane porosity and induce the release of nitrogen-rich metabolites from nitrogen-fixing {F}rankia},
  author = {{C}arro, {L}. and {P}ujic, {P}. and {A}lloisio, {N}. and {F}ournier, {P}. and {B}oubakri, {H}. and {H}ay, {A}. {E}. and {P}oly, {F}. and {F}rancois, {P}hilippe and {H}ocher, {V}al{\'e}rie and {M}ergaert, {P}. and {B}almand, {S}. and {R}ey, {M}. and {H}eddi, {A}. and {N}ormand, {P}.},
  editor = {},
  language = {{ENG}},
  abstract = {{A}ctinorhizal plant growth in pioneer ecosystems depends on the symbiosis with the nitrogen-fixing actinobacterium {F}rankia cells that are housed in special root organs called nodules. {N}itrogen fixation occurs in differentiated {F}rankia cells known as vesicles. {V}esicles lack a pathway for assimilating ammonia beyond the glutamine stage and are supposed to transfer reduced nitrogen to the plant host cells. {H}owever, a mechanism for the transfer of nitrogen-fixation products to the plant cells remains elusive. {H}ere, new elements for this metabolic exchange are described. {W}e show that {A}lnus glutinosa nodules express defensin-like peptides, and one of these, {A}g5, was found to target {F}rankia vesicles. {I}n vitro and in vivo analyses showed that {A}g5 induces drastic physiological changes in {F}rankia, including an increased permeability of vesicle membranes. {A} significant release of nitrogen-containing metabolites, mainly glutamine and glutamate, was found in {N}-2-fixing cultures treated with {A}g5. {T}his work demonstrates that the {A}g5 peptide is central for {F}rankia physiology in nodules and uncovers a novel cellular function for this large and widespread defensin peptide family.},
  keywords = {{FRANCE}},
  booktitle = {},
  journal = {{ISME} {J}ournal},
  volume = {9},
  numero = {8},
  pages = {1723--1733},
  ISSN = {1751-7362},
  year = {2015},
  DOI = {10.1038/ismej.2014.257},
  URL = {https://www.documentation.ird.fr/hor/fdi:010064843},
}