Iron limitation by transferrin promotes simultaneous cheating of pyoverdine and exoprotease in Pseudomonas aeruginosa
Por:
Tostado-Islas, Oswaldo, Mendoza-Ortiz, Alberto, Ramirez-Garcia, Gabriel, Cabrera-Takane, Isamu Daniel, Loarca, Daniel, Perez-Gonzalez, Caleb, Jasso-Chavez, Ricardo, Jimenez-Cortes, J. Guillermo, Hoshiko, Yuki, Maeda, Toshinari, Cazares, Adrian, Garcia-Contreras, Rodolfo
Publicada:
1 ago 2021
Ahead of Print:
1 mar 2021
Resumen:
Pseudomonas aeruginosa is a primary bacterial model to study cooperative
behaviors because it yields exoproducts such as siderophores and
exoproteases that act as public goods and can be exploited by selfish
nonproducers behaving as social cheaters. Iron-limited growth medium,
mainly casamino acids medium supplemented with transferrin, is typically
used to isolate and study nonproducer mutants of the siderophore
pyoverdine. However, using a protein as the iron chelator could
inadvertently select mutants unable to produce exoproteases, since these
enzymes can degrade the transferrin to facilitate iron release. Here we
investigated the evolutionary dynamics of pyoverdine and exoprotease
production in media in which iron was limited by using either
transferrin or a cation chelating resin. We show that concomitant loss
of pyoverdine and exoprotease production readily develops in media
containing transferrin, whereas only pyoverdine loss emerges in medium
treated with the resin. Characterization of exoprotease- and
pyoverdine-less mutants revealed loss in motility, different mutations,
and large genome deletions (13-33 kb) including Quorum Sensing (lasR,
rsal, and lasI) and flagellar genes. Our work shows that using
transferrin as an iron chelator imposes simultaneous selective pressure
for the loss of pyoverdine and exoprotease production. The unintended
effect of transferrin uncovered by our experiments can help to inform
the design of similar studies.
Filiaciones:
Univ Nacl Autonoma Mexico, Fac Med, Dept Microbiol & Parasitol, Mexico City, DF, Mexico
Inst Nacl Cardiol, Dept Bioquim, Mexico City, DF, Mexico
Kyushu Inst Technol, Dept Biol Funct Engn, Kitakyushu, Fukuoka, Japan
EMBLs European Bioinformat Inst EMBL EBI, Wellcome Genome Campus, Cambridge, England
Wellcome Sanger Inst, Wellcome Genome Campus, Cambridge, England
Green Submitted
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