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YeeJ is an inverse autotransporter from Escherichia coli that binds to peptidoglycan and promotes biofilm formation

Identifieur interne : 000029 ( Main/Exploration ); précédent : 000028; suivant : 000030

YeeJ is an inverse autotransporter from Escherichia coli that binds to peptidoglycan and promotes biofilm formation

Auteurs : Marta Martinez-Gil [Espagne] ; Kelvin G. K. Goh ; Elze Rackaityte [États-Unis] ; Chizuko Sakamoto ; Bianca Audrain ; Danilo G. Moriel [Italie] ; Makrina Totsika ; Jean-Marc Ghigo ; Mark A. Schembri ; Christophe Beloin

Source :

RBID : PMC:5595812

Abstract

Escherichia coli is a commensal or pathogenic bacterium that can survive in diverse environments. Adhesion to surfaces is essential for E. coli colonization, and thus it is important to understand the molecular mechanisms that promote this process in different niches. Autotransporter proteins are a class of cell-surface factor used by E. coli for adherence. Here we characterized the regulation and function of YeeJ, a poorly studied but widespread representative from an emerging class of autotransporter proteins, the inverse autotransporters (IAT). We showed that the yeeJ gene is present in ~40% of 96 completely sequenced E. coli genomes and that YeeJ exists as two length variants, albeit with no detectable functional differences. We demonstrated that YeeJ promotes biofilm formation in different settings through exposition at the cell-surface. We also showed that YeeJ contains a LysM domain that interacts with peptidoglycan and thus assists its localization into the outer membrane. Additionally, we identified the Polynucleotide Phosphorylase PNPase as a repressor of yeeJ transcription. Overall, our work provides new insight into YeeJ as a member of the recently defined IAT class, and contributes to our understanding of how commensal and pathogenic E. coli colonise their environments.


Url:
DOI: 10.1038/s41598-017-10902-0
PubMed: 28900103
PubMed Central: 5595812


Affiliations:


Links toward previous steps (curation, corpus...)


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</author>
<author>
<name sortKey="Schembri, Mark A" sort="Schembri, Mark A" uniqKey="Schembri M" first="Mark A." last="Schembri">Mark A. Schembri</name>
<affiliation>
<nlm:aff id="Aff2">
<institution-wrap>
<institution-id institution-id-type="ISNI">0000 0000 9320 7537</institution-id>
<institution-id institution-id-type="GRID">grid.1003.2</institution-id>
<institution>School of Chemistry and Molecular Biosciences, The University of Queensland,</institution>
</institution-wrap>
Brisbane, QLD 4072 Australia</nlm:aff>
<wicri:noCountry code="subfield">QLD 4072 Australia</wicri:noCountry>
</affiliation>
<affiliation>
<nlm:aff id="Aff3">
<institution-wrap>
<institution-id institution-id-type="ISNI">0000 0000 9320 7537</institution-id>
<institution-id institution-id-type="GRID">grid.1003.2</institution-id>
<institution>Australian Infectious Diseases Research Centre, The University of Queensland,</institution>
</institution-wrap>
Brisbane, QLD 4072 Australia</nlm:aff>
<wicri:noCountry code="subfield">QLD 4072 Australia</wicri:noCountry>
</affiliation>
</author>
<author>
<name sortKey="Beloin, Christophe" sort="Beloin, Christophe" uniqKey="Beloin C" first="Christophe" last="Beloin">Christophe Beloin</name>
<affiliation>
<nlm:aff id="Aff1">
<institution-wrap>
<institution-id institution-id-type="ISNI">0000 0001 2353 6535</institution-id>
<institution-id institution-id-type="GRID">grid.428999.7</institution-id>
<institution>Institut Pasteur, Unité de Génétique des Biofilms,</institution>
</institution-wrap>
28 rue du Dr. Roux, 75724 Paris, CEDEX 15 France</nlm:aff>
<wicri:noCountry code="subfield">CEDEX 15 France</wicri:noCountry>
</affiliation>
</author>
</analytic>
<series>
<title level="j">Scientific Reports</title>
<idno type="eISSN">2045-2322</idno>
<imprint>
<date when="2017">2017</date>
</imprint>
</series>
</biblStruct>
</sourceDesc>
</fileDesc>
<profileDesc>
<textClass></textClass>
</profileDesc>
</teiHeader>
<front>
<div type="abstract" xml:lang="en">
<p id="Par1">
<italic>Escherichia coli</italic>
is a commensal or pathogenic bacterium that can survive in diverse environments. Adhesion to surfaces is essential for
<italic>E. coli</italic>
colonization, and thus it is important to understand the molecular mechanisms that promote this process in different niches. Autotransporter proteins are a class of cell-surface factor used by
<italic>E. coli</italic>
for adherence. Here we characterized the regulation and function of YeeJ, a poorly studied but widespread representative from an emerging class of autotransporter proteins, the inverse autotransporters (IAT). We showed that the
<italic>yeeJ</italic>
gene is present in ~40% of 96 completely sequenced
<italic>E. coli</italic>
genomes and that YeeJ exists as two length variants, albeit with no detectable functional differences. We demonstrated that YeeJ promotes biofilm formation in different settings through exposition at the cell-surface. We also showed that YeeJ contains a LysM domain that interacts with peptidoglycan and thus assists its localization into the outer membrane. Additionally, we identified the Polynucleotide Phosphorylase PNPase as a repressor of
<italic>yeeJ</italic>
transcription. Overall, our work provides new insight into YeeJ as a member of the recently defined IAT class, and contributes to our understanding of how commensal and pathogenic
<italic>E. coli</italic>
colonise their environments.</p>
</div>
</front>
<back>
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<li>Californie</li>
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