Lipotoxin F of Pseudomonas aeruginosa is an AlgU-dependent and alginate-independent outer membrane protein involved in resistance to oxidative stress and adhesion to A549 human lung epithelia

Damron, F. Heath; Napper, Jennifer M.; Teter, Mimi; Yu, Hongwei D.

doi:10.1099/mic.0.025833-0

Cited by 35 publications

(34 citation statements)

References 48 publications

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“…PA1119 (YfiB) is an OM lipoprotein recently described to mediate the cyclic-di-GMP-dependent conversion of P. aeruginosa to a small-colony variant phenotype (Malone et al, 2010). The last protein, LptF, has been found to be regulated by the alternative sigma factor AlgU, as will be mentioned later (Damron et al, 2009). It is also worth mentioning that this PG-binding domain is found in non-lipoprotein OM porins such as OprF (Rawling et al, 1998).…”

Section: Peptidoglycan-binding Lipoproteinsmentioning

confidence: 94%

Genome-wide analysis and literature-based survey of lipoproteins in Pseudomonas aeruginosa

et al. 2010

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Pseudomonas aeruginosa is a Gram-negative opportunistic pathogen able to cause acute or chronic infections. Like all other Pseudomonas species, P. aeruginosa has a large genome, >6 Mb, encoding more than 5000 proteins. Many proteins are localized in membranes, among them lipoproteins, which can be found tethered to the inner or the outer membrane. Lipoproteins are translocated from the cytoplasm and their N-terminal signal peptide is cleaved by the signal peptidase II, which recognizes a specific sequence called the lipobox just before the first cysteine of the mature lipoprotein. A majority of lipoproteins are transported to the outer membrane via the LolCDEAB system, while those having an avoidance signal remain in the inner membrane. In Escherichia coli, the presence of an aspartate residue after the cysteine is sufficient to cause the lipoprotein to remain in the inner membrane, while in P. aeruginosa the situation is more complex and involves amino acids at position +3 and +4 after the cysteine. Previous studies indicated that there are 185 lipoproteins in P. aeruginosa, with a minority in the inner membrane. A reanalysis led to a reduction of this number to 175, while new retention signals could be predicted, increasing the percentage of inner-membrane lipoproteins to 20 %. About one-third (62 out of 175) of the lipoprotein genes are present in the 17 Pseudomonas genomes sequenced, meaning that these genes are part of the core genome of the genus. Lipoproteins can be classified into families, including those outer-membrane proteins having a structural role or involved in efflux of antibiotics. Comparison of various microarray data indicates that exposure to epithelial cells or some antibiotics, or conversion to mucoidy, has a major influence on the expression of lipoprotein genes in P. aeruginosa.

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Section: Peptidoglycan-binding Lipoproteinsmentioning

confidence: 94%

Genome-wide analysis and literature-based survey of lipoproteins in Pseudomonas aeruginosa

et al. 2010

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“…In Pseudomonas aeruginosa, ECF sigma factor AlgU responds to environmental stresses with the production of alginate, a component of its meshwork-like structures [30]. The antisigma factor MucA is a negative regulator of alginate production that sequesters AlgU to the inner membrane [31]. In this study, we attempted to find genes on DY-18 genome highly homologous to well-known biofilmassociated genes of S. aureus and P. aeruginosa.…”

Section: Sigma Factors and Two-component Systems On Dy-18mentioning

confidence: 99%

Complete Genome Sequence of Rothia mucilaginosa DY-18: A Clinical Isolate with Dense Meshwork-Like Structures from a Persistent Apical Periodontitis Lesion

et al. 2010

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Rothia mucilaginosa is an opportunistic pathogen in the human oral cavity and pharynx. We found that R. mucilaginosa DY-18, a clinical isolate from a persistent apical periodontitis lesion, had biofilm-like structures. Similar structures were also observed on R. mucilaginosa ATCC25296. To further study these structures, we determined the complete genome sequence of DY-18 and found it a 2.26-Mb chromosome. Regarding stress responsive systems known to affect biofilm formation in many bacteria, DY-18 genome possessed only two sigma factor genes. One of these encoded an additional sigma factor whose promoter-binding activity may be regulated in response to environmental stimuli. Additionally, several genes assigned to two-component signal transduction systems were presented in this genome. To the best of our knowledge, this is the first complete genome of R. mucilaginosa species and our data raise the possibility that this organism regulates the biofilm phenotype through these stress responsive systems.

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“…However, no significant change in either lasI or lasR expression was observed in the transcriptome analysis (Table 2). Previously, we noted a high number of QS-regulated proteins identified in the kinB mutant (11). The transcriptome analysis revealed a large number of QS-regulated genes with increased expression levels in the PAO1 kinB ⌬rpoN strain ( Table 2).…”

Section: Rpon Negatively Regulates Pyochelin Synthesismentioning

confidence: 99%

Analysis of the Pseudomonas aeruginosa Regulon Controlled by the Sensor Kinase KinB and Sigma Factor RpoN

et al. 2012

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f Alginate overproduction by Pseudomonas aeruginosa, also known as mucoidy, is associated with chronic endobronchial infections in cystic fibrosis. Alginate biosynthesis is initiated by the extracytoplasmic function sigma factor ( 22 ; AlgU/AlgT). In the wild-type (wt) nonmucoid strains, such as PAO1, AlgU is sequestered to the cytoplasmic membrane by the anti-sigma factor MucA that inhibits alginate production. One mechanism underlying the conversion to mucoidy is mutation of mucA. However, the mucoid conversion can occur in wt mucA strains via the degradation of MucA by activated intramembrane proteases AlgW and/or MucP. Previously, we reported that the deletion of the sensor kinase KinB in PAO1 induces an AlgW-dependent proteolysis of MucA, resulting in alginate overproduction. This type of mucoid induction requires the alternate sigma factor RpoN ( 54 ). To determine the RpoN-dependent KinB regulon, microarray and proteomic analyses were performed on a mucoid kinB mutant and an isogenic nonmucoid kinB rpoN double mutant. In the kinB mutant of PAO1, RpoN controlled the expression of approximately 20% of the genome. In addition to alginate biosynthetic and regulatory genes, KinB and RpoN also control a large number of genes including those involved in carbohydrate metabolism, quorum sensing, iron regulation, rhamnolipid production, and motility. In an acute pneumonia murine infection model, BALB/c mice exhibited increased survival when challenged with the kinB mutant relative to survival with PAO1 challenge. Together, these data strongly suggest that KinB regulates virulence factors important for the development of acute pneumonia and conversion to mucoidy.

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Lipotoxin F of Pseudomonas aeruginosa is an AlgU-dependent and alginate-independent outer membrane protein involved in resistance to oxidative stress and adhesion to A549 human lung epithelia

Cited by 35 publications

References 48 publications

Genome-wide analysis and literature-based survey of lipoproteins in Pseudomonas aeruginosa

Genome-wide analysis and literature-based survey of lipoproteins in Pseudomonas aeruginosa

Complete Genome Sequence of Rothia mucilaginosa DY-18: A Clinical Isolate with Dense Meshwork-Like Structures from a Persistent Apical Periodontitis Lesion

Analysis of the Pseudomonas aeruginosa Regulon Controlled by the Sensor Kinase KinB and Sigma Factor RpoN

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