Biogenesis of the Gram-Negative Bacterial Outer Membrane

Bos, Martine P.; Robert, Viviane; Tommassen, Jan

doi:10.1146/annurev.micro.61.080706.093245

Cited by 431 publications

(475 citation statements)

References 125 publications

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“…However, since the mechanism of release of cleaved passenger from the cells is not understood, the basis of the influence of SurA on this late step remains obscure. The general periplasmic chaperones Skp and DegP have also been implicated in targeting of OMPs to the Bam complex, operating in a pathway that runs parallel to the main SurA pathway (Bos et al, 2007;Sklar et al, 2007). Our data indicate that both DegP and Skp are dispensable for Hbp biogenesis and secretion (Jong et al, 2007; Supplementary Fig.…”

Section: Bama and Sura Are Required For Secretion Of Hbpmentioning

confidence: 70%

“…Interestingly, BamA and BamB participate in a recently identified machinery that is involved in the insertion of OMPs (Bos et al, 2007;Ruiz et al, 2006). OmpA is an abundant OMP [~300,000 copies per cell (Movva et al, 1980)] with a large periplasmic domain that is similar to the C-terminal domain of RmpM from N. meningitidis, a protein described to be associated with the Bam machinery The Bam complex is involved in secretion of Hbp in this species (Bos et al, 2007).…”

Section: The Hbp110c/348c Translocation Intermediate Is Adjacent To Smentioning

confidence: 99%

“…OmpA is an abundant OMP [~300,000 copies per cell (Movva et al, 1980)] with a large periplasmic domain that is similar to the C-terminal domain of RmpM from N. meningitidis, a protein described to be associated with the Bam machinery The Bam complex is involved in secretion of Hbp in this species (Bos et al, 2007). A role of RmpM or OmpA in OMP biogenesis has not been reported.…”

Section: The Hbp110c/348c Translocation Intermediate Is Adjacent To Smentioning

confidence: 99%

“…This is difficult to reconcile with the cross-links to SurA and BamA. BamA is thought to transiently associate with nascent OMPs delivered by SurA or Skp to mediate their insertion and folding (Bos et al, 2007;Ruiz et al, 2006). The periplasmic POTRA domains in BamA have been implicated in recognition of the Cterminal signature OMP motif, which is also present in Hbp, and nascent b-strands of OMPs (Robert et al, 2006).…”

Section: The Hbp110c/348c Translocation Intermediate Is Adjacent To Smentioning

confidence: 99%

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The Bam (Omp85) complex is involved in secretion of the autotransporter haemoglobin protease

et al. 2009

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Autotransporters are large virulence factors secreted by Gram-negative bacteria. They are synthesized with a C-terminal domain that forms a b-barrel pore in the outer membrane implicated in translocation of the upstream 'passenger' domain across the outer membrane. However, recent structural data suggest that the diameter of the b-barrel pore is not sufficient to allow the passage of partly folded structures observed for several autotransporters. Here, we have used a stalled translocation intermediate of the autotransporter Hbp to identify components involved in insertion and translocation of the protein across the outer membrane. At this intermediate stage the b-domain was not inserted and folded as an integral b-barrel in the outer membrane whereas part of the passenger was surface exposed. The intermediate was copurified with the periplasmic chaperone SurA and subunits of the Bam (Omp85) complex that catalyse the insertion and assembly of outer-membrane proteins. The data suggest a critical role for this general machinery in the translocation of autotransporters across the outer membrane.

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Section: Bama and Sura Are Required For Secretion Of Hbpmentioning

confidence: 70%

Section: The Hbp110c/348c Translocation Intermediate Is Adjacent To Smentioning

confidence: 99%

Section: The Hbp110c/348c Translocation Intermediate Is Adjacent To Smentioning

confidence: 99%

Section: The Hbp110c/348c Translocation Intermediate Is Adjacent To Smentioning

confidence: 99%

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The Bam (Omp85) complex is involved in secretion of the autotransporter haemoglobin protease

et al. 2009

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“…1. Anchoring of the lipid motif in the outer membrane of the bacteria exposes the polypeptide to the bacterial cell surface, thus making it accessible to bactericidal antibodies directed to the protein (15).…”

Section: Introductionmentioning

confidence: 99%

The Dual Role of Lipids of the Lipoproteins in Trumenba, a Self-Adjuvanting Vaccine Against Meningococcal Meningitis B Disease

Luo

Friese

Runnels

et al. 2016

AAPS J

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ABSTRACT.Trumenba (bivalent rLP2086) is a vaccine licensed for the prevention of meningococcal meningitis disease caused by Neisseria meningitidis serogroup B (NmB) in individuals 10-25 years of age in the USA. The vaccine is composed of two factor H binding protein (fHbp) variants that were recombinantly expressed in Escherichia coli as native lipoproteins: rLP2086-A05 and rLP2086-B01. The vaccine was shown to induce potent bactericidal antibodies against a broad range of NmB isolates expressing fHbp that were different in sequence from the fHbp vaccine antigens. Here, we describe the characterization of the vaccine antigens including the elucidation of their structure which is characterized by two distinct motifs, the polypeptide domain and the N-terminal lipid moiety. In the vaccine formulation, the lipoproteins self-associate to form micelles driven by the hydrophobicity of the lipids and limited by the size of the folded polypeptides. The micelles help to increase the structural stability of the lipoproteins in the absence of bacterial cell walls. Analysis of the lipoproteins in Toll-like receptor (TLR) activation assays revealed their TLR2 agonist activity. This activity was lost with removal of the O-linked fatty acids, similar to removal of all lipids, demonstrating that this moiety plays an adjuvant role in immune activation. The thorough understanding of the structure and function of each moiety of the lipoproteins, as well as their relationship, lays the foundation for identifying critical parameters to guide vaccine development and manufacture.

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Efflux Pumps of Gram‐Negative Bacteria: Genetic Responses to Stress and the Modulation of their Activity by pH, Inhibitors, and Phenothiazines

Amaral¹,

Fanning²,

Pagès³

2011

Advances in Enzymology - And Related Areas of Molecular Biology

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Biogenesis of the Gram-Negative Bacterial Outer Membrane

Cited by 431 publications

References 125 publications

The Bam (Omp85) complex is involved in secretion of the autotransporter haemoglobin protease

The Bam (Omp85) complex is involved in secretion of the autotransporter haemoglobin protease

The Dual Role of Lipids of the Lipoproteins in Trumenba, a Self-Adjuvanting Vaccine Against Meningococcal Meningitis B Disease

Efflux Pumps of Gram‐Negative Bacteria: Genetic Responses to Stress and the Modulation of their Activity by pH, Inhibitors, and Phenothiazines

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