Type V Secretion Systems in Bacteria

Fan, Enguo; Chauhan, Nandini; Udatha, D.B.R.K. Gupta; Leo, Jack C.; Linke, Dirk

doi:10.1128/9781555819286.ch11

Cited by 27 publications

(30 citation statements)

References 172 publications

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“…Our mutagenesis scheme was based on the expectation that surface‐exposed arginine residues would perturb the membrane insertion reaction per se but, unlike previously studied mutations (CastilloKeller and Misra, ; Wzorek et al ., ), would not grossly impair protein folding. Whereas OmpLA consists solely of a 12‐stranded β barrel (Snijder et al ., ), EspP is a member of the autotransporter superfamily that contains a large N‐terminal extracellular (passenger) domain in addition to a C‐terminal 12‐stranded β barrel domain (Dautin and Bernstein, ; Fan et al ., ). Although the passenger domain is released by proteolytic cleavage following its translocation across the OM, the two domains are initially connected by a segment that passes through the β barrel pore (Dautin et al ., ; Barnard et al ., ).…”

Section: Introductionmentioning

confidence: 97%

Selective pressure for rapid membrane integration constrains the sequence of bacterial outer membrane proteins

Peterson

Plummer

Fleming

et al. 2017

Molecular Microbiology

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SUMMARY Almost all bacterial outer membrane proteins (OMPs) contain a β barrel domain that serves as a membrane anchor, but the assembly and quality control of these proteins are poorly understood. Here we show that the introduction of a single lipid-facing arginine residue near the middle of the β barrel of the E. coli OMPs OmpLA and EspP creates an energy barrier that impedes membrane insertion. Although several unintegrated OmpLA mutants remained insertion-competent, they were slowly degraded by the periplasmic protease DegP. Two EspP mutants were also gradually degraded by DegP, but were toxic because they first bound to the Bam complex, an essential heteroligomer that catalyzes the membrane insertion of OMPs. Interestingly, another EspP mutant likewise formed a prolonged, deleterious interaction with the Bam complex, but was protected from degradation and eventually inserted into the membrane in a native conformation. The different types of interactions between the EspP mutants and the Bam complex that we observed may correspond to distinct stages in OMP assembly. Our results show that sequences that significantly delay assembly are disfavored not only because unintegrated OMPs are subject to degradation, but also because OMPs that assemble slowly can form dominant-negative interactions with the Bam complex.

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Section: Introductionmentioning

confidence: 97%

Selective pressure for rapid membrane integration constrains the sequence of bacterial outer membrane proteins

Peterson

Plummer

Fleming

et al. 2017

Molecular Microbiology

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“…Type III and type IV protein secretion systems often involved in effector protein injection in hosts are lacking in strain BH72 (Krause et al ., ); however, two type VI and one type V secretion systems are present. Type V secretion denotes a variety of secretion systems that cross the outer membrane in Gram‐negative bacteria but that depend on the Sec machinery for transport through the inner membrane (Fan et al ., ). Their seemingly autonomous transport through the outer membrane has led to the term ‘autotransporters’ for various subclasses of type V secretion.…”

Section: Introductionmentioning

confidence: 97%

Global expression analysis of the response to microaerobiosis reveals an important cue for endophytic establishment of Azoarcus sp. BH72

Sarkar

Marszałkowska

Schäfer

et al. 2016

Environmental Microbiology

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The endophyte Azoarcus sp. BH72, fixing nitrogen microaerobically, encounters low O tensions in flooded roots. Therefore, its transcriptome upon shift to microaerobiosis was analyzed using oligonucleotide microarrays. A total of 8.7% of the protein-coding genes were significantly modulated. Aerobic conditions induced expression of genes involved in oxidative stress protection, while under microaerobiosis, 233 genes were upregulated, encoding hypothetical proteins, transcriptional regulators, and proteins involved in energy metabolism, among them a cbb -type terminal oxidase contributing to but not essential for N fixation. A newly established sensitive transcriptional reporter system using tdTomato allowed to visualize even relatively low bacterial gene expression in association with roots. Beyond metabolic changes, low oxygen concentrations seemed to prime transcription for plant colonization: Several genes known to be required for endophytic rice interaction were induced, and novel bacterial colonization factors were identified, such as azo1653. The cargo of the type V autotransporter Azo1653 had similarities to the attachment factor pertactin. Although for short term swarming-dependent colonization, it conferred a competitive disadvantage, it contributed to endophytic long-term establishment inside roots. Proteins sharing such opposing roles in the colonization process appear to occur more generally, as we demonstrated a very similar phenotype for another attachment protein, Azo1684. This suggests distinct cellular strategies for endophyte establishment.

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“…The topography whereby an extracellular passenger domain is displayed via a transmembrane β‐barrel assembled into the cell surface is the defining feature of a Type 5 secretion system. Currently there are at least six subtypes (Bleves et al., ; Fan, Chauhan, Udatha, Leo, & Linke, ; Heinz et al., ; Leo, Oberhettinger, Schutz, & Linke, ) distinguished by the β‐barrel domain used as the protein translocation device: autotransporters (Type Va), two‐partner secretion systems (Type Vb), trimeric autotransporters (Type Vc), patatins (Type Vd), inverse‐autotransporters (Type Ve) and two‐partner inverse‐autotransporters (Type Vf). The Hp_OMP families of Hop and Hor proteins would constitute the first subtype of the Type 5 secretion system to be exclusive to a single genus of bacteria.…”

Section: Discussionmentioning

confidence: 99%

Reductive evolution in outer membrane protein biogenesis has not compromised cell surface complexity in Helicobacter pylori

et al. 2017

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Helicobacter pylori is a gram‐negative bacterial pathogen that chronically inhabits the human stomach. To survive and maintain advantage, it has evolved unique host–pathogen interactions mediated by Helicobacter‐specific proteins in the bacterial outer membrane. These outer membrane proteins (OMPs) are anchored to the cell surface via a C‐terminal β‐barrel domain, which requires their assembly by the β‐barrel assembly machinery (BAM). Here we have assessed the complexity of the OMP C‐terminal β‐barrel domains employed by H. pylori, and characterized the H. pylori BAM complex. Around 50 Helicobacter‐specific OMPs were assessed with predictive structural algorithms. The data suggest that H. pylori utilizes a unique β‐barrel architecture that might constitute H. pylori‐specific Type V secretions system. The structural and functional diversity in these proteins is encompassed by their extramembrane domains. Bioinformatic and biochemical characterization suggests that the low β‐barrel‐complexity requires only minimalist assembly machinery. The H. pylori proteins BamA and BamD associate to form a BAM complex, with features of BamA enabling an oligomerization that might represent a mechanism by which a minimalist BAM complex forms a larger, sophisticated machinery capable of servicing the outer membrane proteome of H. pylori.

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Type V Secretion Systems in Bacteria

Cited by 27 publications

References 172 publications

Selective pressure for rapid membrane integration constrains the sequence of bacterial outer membrane proteins

Selective pressure for rapid membrane integration constrains the sequence of bacterial outer membrane proteins

Global expression analysis of the response to microaerobiosis reveals an important cue for endophytic establishment of Azoarcus sp. BH72

Reductive evolution in outer membrane protein biogenesis has not compromised cell surface complexity in Helicobacter pylori

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