Versatile in vitro system to study translocation and functional integration of bacterial outer membrane proteins

Norell, Derrick; Heuck, Alexander; Tran‐Thi, Thuy‐Anh; Götzke, Hansjörg; Jacob‐Dubuisson, Françoise; Clausen, Tim; Daley, Daniel O.; Braun, Volkmar; Müller, Matthias; Fan, Enguo

doi:10.1038/ncomms6396

Cited by 27 publications

(42 citation statements)

References 47 publications

(71 reference statements)

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“…The N-terminal region also contains the TPS transport domain (also known as the hemagglutinin activation domain, PF05860), which is required for export across the outer membrane. CdiB recognizes the TPS transport domain as it emerges into the periplasm and transports CdiA through the central pore in its β-barrel domain 21; 32; 33 . CdiA proteins also share FHA-1 (PF05594) and FHA-2 (PF13332) peptide repeats with FHA/FhaB (Fig.…”

Section: Architecture Of Cdia Effector Proteinsmentioning

confidence: 99%

Contact-Dependent Growth Inhibition (CDI) and CdiB/CdiA Two-Partner Secretion Proteins

Willett

Ruhe

Goulding

et al. 2015

Journal of Molecular Biology

108

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Bacteria have developed several strategies to communicate and compete with one another in complex environments. One important mechanism of inter-bacterial competition is contact-dependent growth inhibition (CDI), in which some Gram-negative bacteria use CdiB/CdiA two-partner secretion proteins to suppress the growth of neighboring target cells. CdiB is an Omp85 outer-membrane protein that exports and assembles CdiA exoproteins onto the inhibitor-cell surface. CdiA binds to receptors on susceptible bacteria and subsequently delivers its C-terminal toxin domain (CdiA-CT) into the target cell. CDI systems also encode CdiI immunity proteins, which specifically bind to the CdiA-CT and neutralize its toxin activity, thereby protecting CDI+ cells from auto-inhibition. Remarkably, CdiA-CT sequences are highly variable between bacteria, as are the corresponding CdiI immunity proteins. Variations in CDI toxin/immunity proteins suggest that these systems function in bacterial self/nonself recognition and thereby play an important role in microbial communities. In this review, we discuss recent advances in the biochemistry, structural biology and physiology of CDI.

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Section: Architecture Of Cdia Effector Proteinsmentioning

confidence: 99%

Contact-Dependent Growth Inhibition (CDI) and CdiB/CdiA Two-Partner Secretion Proteins

Willett

Ruhe

Goulding

et al. 2015

Journal of Molecular Biology

108

View full text Add to dashboard Cite

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“…Mutation of the tamAB genes impacts on cell-surface expression of the AT proteins Ag43, EhaA and the plasmid encoded C. rodentium putative AT, p1112 (Selkrig et al, 2012). The BAM complex has also been shown to contribute to the translocation of Ag43 and EspP (Norell et al, 2014).…”

Section: Discussionmentioning

confidence: 99%

“…Indeed both complexes have previously been shown to assist in Ag43 surface expression (Selkrig et al, 2012, Norell et al, 2014 Despite the vast array of functions associated with AT proteins, the translocation of these proteins appears to be conserved among UPEC and other Gram-negative pathogens. The periplasmic chaperones SurA, Skp, DegP and FkpA are known to bind to AT proteins and assist in their translocation (Ruiz-Perez et al, 2009, Ieva and Bernstein, 2009a.…”

Section: Growth Characteristics Of Mg1655 Periplasmic Chaperone Mutanmentioning

confidence: 99%

“…All five BAM proteins were recently shown to contribute to the translocation of both Ag43 and EspP into the membrane of proteoliposomes (Norell et al, 2014, RomanHernandez et al, 2014. Furthermore, the TAM also aids in the translocation of Ag43 in E.…”

Section: Growth Characteristics Of Mg1655 Periplasmic Chaperone Mutanmentioning

confidence: 99%

“…The expression of fimbriae contributes to UPEC virulence by aiding in initial attachment to urothelial cells. UPEC possess multiple types of fimbriae, including type 1 fimbriae (cystitis associated), P fimbriae (pyelonephritis associated) and S/ F1C fimbriae (Rahdar et al, 2014, Blanco et al, 1997, Toval et al, 2014, Norinder et al, 2012. Type 1 and P fimbriae represent the two best studied fimbriae present in UPEC.…”

Section: Fimbrial Adhesinsmentioning

confidence: 99%

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Autotransporter proteins of Uropathogenic Escherichia coli: regulation, characterisation and the role of periplasmic proteins in their expression

Nichols¹

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Uropathogenic Escherichia coli (UPEC) are the primary cause for all urinary tract infections.Autotransporter (AT) proteins are virulence factors secreted by the type V secretion pathway. This project examined the prevalence, regulation and expression of the vacuolating AT toxin (Vat), and the role of periplasmic chaperone proteins in AT translocation.The vacuolating autotransporter (AT) toxin (Vat) contributes to Uropathogenic Escherichia coli (UPEC) fitness during systemic infection. Vat is a serine protease AT of Enterobacteriaceae (SPATE) with cytotoxic activity. Here we characterised Vat and investigated its regulation in UPEC.We assessed the prevalence of vat in a collection of 45 UPEC urosepsis strains and showed it that was present in 31 (68%) of the isolates. The isolates containing the vat gene corresponded to three major E. coli sequence types (ST12, 73 and 95) and these strains secreted the Vat protein.Further analysis of the vat genetic locus identified a conserved gene located directly downstream of vat that encodes a putative MarR-like transcriptional regulator, which we termed vatX. The vatvatX genes were present in the UPEC reference strain CFT073 and RT-PCR revealed both genes are co-transcribed. Over-expression of vatX in CFT073 led to a 3-fold increase in vat gene transcription. The vat promoter region contained three putative nucleation sites for the global transcriptional regulator H-NS; thus the hns gene was mutated in CFT073 (to generate CFT073hns).Western blot analysis using a Vat-specific antibody revealed a significant increase in Vat expression in CFT073hns compared to wild-type CFT073. Direct H-NS binding to the vat promoter region was demonstrated using purified H-NS in combination with electrophoresis mobility shift assays. Finally, Vat-specific antibodies were detected in plasma samples from urosepsis patients iv Declaration by authorThis thesis is composed of my original work, and contains no material previously published or written by another person except where due reference has been made in the text. I have clearly stated the contribution by others to jointly-authored works that I have included in my thesis.

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TtOmp85, a single Omp85 member protein functions as a β-barrel protein insertase and an autotransporter translocase without any accessory proteins

Chu

Wang

Weigold

et al. 2021

Biochemical and Biophysical Research Communications

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Versatile in vitro system to study translocation and functional integration of bacterial outer membrane proteins

Cited by 27 publications

References 47 publications

Contact-Dependent Growth Inhibition (CDI) and CdiB/CdiA Two-Partner Secretion Proteins

Contact-Dependent Growth Inhibition (CDI) and CdiB/CdiA Two-Partner Secretion Proteins

Autotransporter proteins of Uropathogenic Escherichia coli: regulation, characterisation and the role of periplasmic proteins in their expression

TtOmp85, a single Omp85 member protein functions as a β-barrel protein insertase and an autotransporter translocase without any accessory proteins

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