The inverse autotransporter family: Intimin, invasin and related proteins

Leo, Jack C.; Oberhettinger, Philipp; Schütz, Monika; Linke, Dirk

doi:10.1016/j.ijmm.2014.12.011

Cited by 65 publications

(74 citation statements)

References 71 publications

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“…The three loci encoding members of the T5eSS subfamily can also be found in E. coli K-12. This family of proteins has been implicated in mediating attachment to host cells [49]. Scrutiny of the distribution of the T5SS genes across the evolutionary spectrum of E. coli reveals no strong association of these genes with pathogenic or non-pathogenic isolates.…”

Section: Resultsmentioning

confidence: 99%

Sequencing a piece of history: complete genome sequence of the original Escherichia coli strain

et al. 2017

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In 1885, Theodor Escherich first described the Bacillus coli commune, which was subsequently renamed Escherichia coli. We report the complete genome sequence of this original strain (NCTC 86). The 5 144 392 bp circular chromosome encodes the genes for 4805 proteins, which include antigens, virulence factors, antimicrobial-resistance factors and secretion systems, of a commensal organism from the pre-antibiotic era. It is located in the E. coli A subgroup and is closely related to E. coli K-12 MG1655. E. coli strain NCTC 86 and the non-pathogenic K-12, C, B and HS strains share a common backbone that is largely co-linear. The exception is a large 2 803 932 bp inversion that spans the replication terminus from gmhB to clpB. Comparison with E. coli K-12 reveals 41 regions of difference (577 351 bp) distributed across the chromosome. For example, and contrary to current dogma, E. coli NCTC 86 includes a nine gene sil locus that encodes a silver-resistance efflux pump acquired before the current widespread use of silver nanoparticles as an antibacterial agent, possibly resulting from the widespread use of silver utensils and currency in Germany in the 1800s. In summary, phylogenetic comparisons with other E. coli strains confirmed that the original strain isolated by Escherich is most closely related to the non-pathogenic commensal strains. It is more distant from the root than the pathogenic organisms E. coli 042 and O157 : H7; therefore, it is not an ancestral state for the species.

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Section: Resultsmentioning

confidence: 99%

Sequencing a piece of history: complete genome sequence of the original Escherichia coli strain

et al. 2017

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“…Type Ve proteins are intimins and invasins (Tsai et al, 2010; Leo et al, 2015b; Heinz et al, 2016). In these proteins, the 12-stranded transmembrane β barrel precedes the passenger domain, making them “reverse ATs” (Tsai et al, 2010; Fairman et al, 2012; Oberhettinger et al, 2012).…”

Section: Introduction: An Overview Of Type V Secretionmentioning

confidence: 99%

Two-Partner Secretion: Combining Efficiency and Simplicity in the Secretion of Large Proteins for Bacteria-Host and Bacteria-Bacteria Interactions

Guérin

Bigot

Schneider

et al. 2017

Front. Cell. Infect. Microbiol.

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Initially identified in pathogenic Gram-negative bacteria, the two-partner secretion (TPS) pathway, also known as Type Vb secretion, mediates the translocation across the outer membrane of large effector proteins involved in interactions between these pathogens and their hosts. More recently, distinct TPS systems have been shown to secrete toxic effector domains that participate in inter-bacterial competition or cooperation. The effects of these systems are based on kin vs. non-kin molecular recognition mediated by specific immunity proteins. With these new toxin-antitoxin systems, the range of TPS effector functions has thus been extended from cytolysis, adhesion, and iron acquisition, to genome maintenance, inter-bacterial killing and inter-bacterial signaling. Basically, a TPS system is made up of two proteins, the secreted TpsA effector protein and its TpsB partner transporter, with possible additional factors such as immunity proteins for protection against cognate toxic effectors. Structural studies have indicated that TpsA proteins mainly form elongated β helices that may be followed by specific functional domains. TpsB proteins belong to the Omp85 superfamily. Open questions remain on the mechanism of protein secretion in the absence of ATP or an electrochemical gradient across the outer membrane. The remarkable dynamics of the TpsB transporters and the progressive folding of their TpsA partners at the bacterial surface in the course of translocation are thought to be key elements driving the secretion process.

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“…Ail is furthermore required for full virulence of Y. pestis and the delivery of pathogenicity factors into host cells (9)(10)(11)(12). The invasin subfamily comprises adhesins of the inverse autotransporter group also referred to as type Ve secretion system (13,14). InvA represents the prototype of the large bacterial invasin subfamily of adhesins (reviewed in (2,3,13)).…”

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confidence: 99%

“…The invasin subfamily comprises adhesins of the inverse autotransporter group also referred to as type Ve secretion system (13,14). InvA represents the prototype of the large bacterial invasin subfamily of adhesins (reviewed in (2,3,13)). InvA is the major adhesion factor of Y. pseudotuberculosis and is sufficient to promote tight binding to cells by exploiting β1 integrins as cellular receptors (15).…”

mentioning

confidence: 99%

The invasin D protein from Yersinia pseudotuberculosis selectively binds the Fab region of host antibodies and affects colonization of the intestine

Sadana

Geyer

Pezoldt

et al. 2018

Journal of Biological Chemistry

574

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The inverse autotransporter family: Intimin, invasin and related proteins

Cited by 65 publications

References 71 publications

Sequencing a piece of history: complete genome sequence of the original Escherichia coli strain

Sequencing a piece of history: complete genome sequence of the original Escherichia coli strain

Two-Partner Secretion: Combining Efficiency and Simplicity in the Secretion of Large Proteins for Bacteria-Host and Bacteria-Bacteria Interactions

The invasin D protein from Yersinia pseudotuberculosis selectively binds the Fab region of host antibodies and affects colonization of the intestine

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