CexE Is A Virulence Factor of<i>Citrobacter rodentium</i>And Present In Enteric Pathogens Of Humans

Rivas, Zachary P.; Rm, McCormack; Adkins, Becky; Munson, George P.

doi:10.1101/375527

Cited by 1 publication

(2 citation statements)

References 45 publications

(48 reference statements)

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“…In these studies, Aap-mCherry was accumulated in the periplasmic poles of 042aatD and colocalized with the bacterial membrane in 042aap, which bears a functional AatD (Fig 6H-6L and S3 Fig). Regarding the percentage of bacteria expressing Aap at the bacterial surface, a study using the homologous Aap of C. rodentium CexE found similar results, not all bacteria export CexE to the bacterial surface [37].…”

Section: Plos Pathogensmentioning

confidence: 83%

“…Since Aap homologs are expressed within virulence regulons of several species of enteric pathogens and required for colonization of murine intestinal tissues by C. rodentium in vivo [37]. We sought to determine if affecting Aap trafficking to the external milieu in 042aatD could affect bacterial colonization using the streptomycin-treated mouse model (ST-model) [38].…”

Section: Evaluation Of 04aatd Mutant In the Streptomycin-treated Mousmentioning

confidence: 99%

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Characterization of a novel AraC/XylS-regulated family of N-acyltransferases in pathogens of the order Enterobacterales

et al. 2020

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Enteroaggregative Escherichia coli (EAEC) is a diarrheagenic pathotype associated with traveler's diarrhea, foodborne outbreaks and sporadic diarrhea in industrialized and developing countries. Regulation of virulence in EAEC is mediated by AggR and its negative regulator Aar. Together, they control the expression of at least 210 genes. On the other hand, we observed that about one third of Aar-regulated genes are related to metabolism and transport. In this study we show the AggR/Aar duo controls the metabolism of lipids. Accordingly, we show that AatD, encoded in the AggR-regulated aat operon (aatPABCD) is an N-acyltransferase structurally similar to the essential Apolipoprotein N-acyltransferase Lnt and is required for the acylation of Aap (anti-aggregation protein). Deletion of aatD impairs posttranslational modification of Aap and causes its accumulation in the bacterial periplasm. trans-complementation of 042aatD mutant with the AatD homolog of ETEC or with the Nacyltransferase Lnt reestablished translocation of Aap. Site-directed mutagenesis of the E207 residue in the putative acyltransferase catalytic triad disrupted the activity of AatD and caused accumulation of Aap in the periplasm due to reduced translocation of Aap at the bacterial surface. Furthermore, Mass spectroscopy revealed that Aap is acylated in a putative lipobox at the N-terminal of the mature protein, implying that Aap is a lipoprotein. Lastly, deletion of aatD impairs bacterial colonization of the streptomycin-treated mouse model. Our findings unveiled a novel N-acyltransferase family associated with bacterial virulence, and that is tightly regulated by AraC/XylS regulators in the order Enterobacterales.

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Section: Plos Pathogensmentioning

confidence: 83%

Section: Evaluation Of 04aatd Mutant In the Streptomycin-treated Mousmentioning

confidence: 99%

Characterization of a novel AraC/XylS-regulated family of N-acyltransferases in pathogens of the order Enterobacterales

et al. 2020

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show abstract

CexE Is A Virulence Factor ofCitrobacter rodentiumAnd Present In Enteric Pathogens Of Humans

Abstract: (250 words) 9

Cited by 1 publication

References 45 publications

Characterization of a novel AraC/XylS-regulated family of N-acyltransferases in pathogens of the order Enterobacterales

Characterization of a novel AraC/XylS-regulated family of N-acyltransferases in pathogens of the order Enterobacterales

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