Small outer-membrane lipoprotein, SmpA, is regulated by σ E and has a role in cell envelope integrity and virulence of Salmonella enterica serovar Typhimurium

Lewis, Claire E.; Škovierová, Henrieta; Rowley, Gary; Řežuchová, Bronislava; Homerová, Dagmar; Stevenson, Andrew; Sherry, Aileen; Kormanec, Ján; Roberts, Mark

doi:10.1099/mic.0.2007/011999-0

Cited by 29 publications

(30 citation statements)

References 37 publications

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“…The membranes of cells lacking BamE contain normal levels of the TolC homologue RsaF (Toporowski et al, 2004), but contain greatly reduced levels of an aggregate of the secretin CpaC (Viollier et al, 2002), as well as three predicted TonBdependent receptors. These results are consistent with the phenotypes of bamE or omlA mutants in other species (Lewis et al, 2008;Ochsner et al, 1999;Sklar et al, 2007). We further show that BamE is required for the timely initiation of stalk biogenesis during the Caulobacter cell division cycle.…”

Section: Introductionsupporting

confidence: 81%

“…Thus, Caulobacter BamE is particularly important to sustain rapid growth on rich medium. Unlike the Caulobacter DbamE mutant, P. aeruginosa, E. coli and S. Typhimurium strains lacking OmlA or BamE have wild-type growth rates in both rich and minimal media (Lewis et al, 2008;Ochsner et al, 1999;Sklar et al, 2007). However, other combinations of mutations that affect components of the BAM complex in E. coli are only tolerated when the growth rate is reduced by propagation on minimal media or at low temperature Wu et al, 2005).…”

Section: Growth Defect Of the Dbame Mutantmentioning

confidence: 99%

“…Mutants in other species lacking components of the BAM complex are hypersensitive to some chemical agents due to membrane permeability defects (Fardini et al, 2009;Lewis et al, 2008;Ochsner et al, 1999;Ruiz et al, 2006;Volokhina et al, 2009). We tested the sensitivity of the wild-type and DbamE Caulobacter strains to a variety of detergents and antibiotics.…”

Section: Heat and Chemical Sensitivity Of The Dbame Mutantmentioning

confidence: 99%

“…Each species whose bamE/omlA mutant has been tested for chemical sensitivity defects displays a different basal level of sensitivity to different detergents and antibiotics (Fardini et al, 2009;Fuangthong et al, 2008;Lewis et al, 2008;Ochsner et al, 1999). For example, wild-type Xanthomonas campestris pv.…”

Section: Heat and Chemical Sensitivity Of The Dbame Mutantmentioning

confidence: 99%

“…However, proteins closely related to CC1365 encoded in other a-proteobacterial genomes have been annotated as members of the SmpA/OmlA family of lipoproteins (Badger et al, 2006;DelVecchio et al, 2002), which is present in the alpha-, beta-and gammaproteobacteria. We aligned the amino acid sequence of CC1365 with BamE and OmlA proteins that have been studied experimentally from the organisms E. coli (Sklar et al, 2007), Salmonella enterica serovar Typhimurium (Lewis et al, 2008), P. aeruginosa PAO1 (Ochsner et al, 1999) and Xanthomonas axonopodis pv. citri (Vanini et al, 2008) using Kalign (Lassmann & Sonnhammer, 2005).…”

Section: Cc1365 Has Homology To the Lipoprotein Bamementioning

confidence: 99%

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The BAM complex subunit BamE (SmpA) is required for membrane integrity, stalk growth and normal levels of outer membrane β-barrel proteins in Caulobacter crescentus

2010

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The outer membrane of Gram-negative bacteria is an essential compartment containing a specific complement of lipids and proteins that constitute a protective, selective permeability barrier. Outer membrane β-barrel proteins are assembled into the membrane by the essential hetero-oligomeric BAM complex, which contains the lipoprotein BamE. We have identified a homologue of BamE, encoded by CC1365, which is located in the outer membrane of the stalked alpha-proteobacterium Caulobacter crescentus. BamE associates with proteins whose homologues in other bacteria are known to participate in outer membrane protein assembly: BamA (CC1915), BamB (CC1653) and BamD (CC1984). Caulobacter cells lacking BamE grow slowly in rich medium and are hypersensitive to anionic detergents, some antibiotics and heat exposure, which suggest that the membrane integrity of the mutant is compromised. Membranes of the ΔbamE mutant have normal amounts of the outer membrane protein RsaF, a TolC homologue, but are deficient in CpaC*, an aggregated form of the outer membrane secretin for type IV pili. ΔbamE membranes also contain greatly reduced amounts of three TonB-dependent receptors that are abundant in wild-type cells. Cells lacking BamE have short stalks and are delayed in stalk outgrowth during the cell cycle. Based on these findings, we propose that Caulobacter BamE participates in the assembly of outer membrane β-barrel proteins, including one or more substrates required for the initiation of stalk biogenesis.

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Section: Introductionsupporting

confidence: 81%

Section: Growth Defect Of the Dbame Mutantmentioning

confidence: 99%

Section: Heat and Chemical Sensitivity Of The Dbame Mutantmentioning

confidence: 99%

Section: Heat and Chemical Sensitivity Of The Dbame Mutantmentioning

confidence: 99%

Section: Cc1365 Has Homology To the Lipoprotein Bamementioning

confidence: 99%

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The BAM complex subunit BamE (SmpA) is required for membrane integrity, stalk growth and normal levels of outer membrane β-barrel proteins in Caulobacter crescentus

2010

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Improved enrichment and proteomic identification of outer membrane proteins from a Gram‐negative bacterium: Focus on Caulobacter crescentus

Cao¹,

Johnson²,

Bazemore‐Walker³

2011

Proteomics

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Efforts to characterize proteins found in the outer membrane (OM) of Gram-negative bacteria have been steadily increasing due to the promise of expanding our understanding of fundamental bacterial processes such as cell adhesion or cell wall biogenesis as well as the promise of finding potential vaccine- or drug-targets for virulent bacteria. We have developed a mass spectrometry-compatible experimental strategy that resulted in increased coverage of the OM proteome of a model organism, Caulobacter crescentus. The specificity of the OM enrichment step was improved by using detergent solubilization of the protein pellet, low-density cell culture conditions, and a surface-layer deficient cell line. Additionally, efficient gel-assisted digestion, high-resolution RP/RP-MS/MS, and rigorous bioinformatic analysis led to the identification of 234 proteins using strict identification criteria (≥ two unique peptides per protein; peptide false discovery rate <2%). Eighty-four of the detected proteins were predicted to localize to the OM or extracellular space. These results represent ~70% coverage of the predicted OM/extracellular proteome of C. crescentus. This analytical approach, which considers important experimental variables not previously explored in published OM protein studies, can be applied to other OM proteomic endeavors "as is" or with slight modification and should improve the large-scale study of this especially challenging subproteome.

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The bacterial outer membrane β‐barrel assembly machinery

Kim¹,

Aulakh²,

Paetzel³

2012

Protein Science

104

113

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b-Barrel proteins found in the outer membrane of Gram-negative bacteria serve a variety of cellular functions. Proper folding and assembly of these proteins are essential for the viability of bacteria and can also play an important role in virulence. The b-barrel assembly machinery (BAM) complex, which is responsible for the proper assembly of b-barrels into the outer membrane of Gram-negative bacteria, has been the focus of many recent studies. This review summarizes the significant progress that has been made toward understanding the structure and function of the bacterial BAM complex.

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Small outer-membrane lipoprotein, SmpA, is regulated by σ E and has a role in cell envelope integrity and virulence of Salmonella enterica serovar Typhimurium

Cited by 29 publications

References 37 publications

The BAM complex subunit BamE (SmpA) is required for membrane integrity, stalk growth and normal levels of outer membrane β-barrel proteins in Caulobacter crescentus

The BAM complex subunit BamE (SmpA) is required for membrane integrity, stalk growth and normal levels of outer membrane β-barrel proteins in Caulobacter crescentus

Improved enrichment and proteomic identification of outer membrane proteins from a Gram‐negative bacterium: Focus on Caulobacter crescentus

The bacterial outer membrane β‐barrel assembly machinery

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