The <scp>I</scp>ntimin periplasmic domain mediates dimerisation and binding to peptidoglycan

Leo, Jack C.; Oberhettinger, Philipp; Chaubey, Manish; Schütz, Monika; Kühner, Daniel; Bertsche, Ute; Schwarz, Heinz; Götz, Friedrich; Autenrieth, Ingo B.; Coles, Murray; Linke, Dirk

doi:10.1111/mmi.12840

Cited by 31 publications

(35 citation statements)

References 52 publications

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“…After transfer, the membranes were blocked with PBS containing 2% w/v skimmed milk powder for 1 h at room temperature with shaking (60 rpm). An anti‐MalE antibody (Leo et al , ) was added diluted 1:10,000 in blocking buffer. After an hour's incubation as above, the membrane was washed twice with PBS‐T (PBS with 0.05% Tween20), after which an anti‐rabbit antibody‐CF ® 770 conjugate (Biotium) was added diluted 1:10,000 in blocking buffer.…”

Section: Methodsmentioning

confidence: 99%

Insights into the autotransport process of a trimeric autotransporter, Yersinia Adhesin A (YadA)

Chauhan

Hatlem

Orwick‐Rydmark

et al. 2019

Molecular Microbiology

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Summary Trimeric autotransporter adhesins (TAAs) are a subset of a larger protein family called the type V secretion systems. They are localized on the cell surface of Gram‐negative bacteria, function as mediators of attachment to inorganic surfaces and host cells, and thus include important virulence factors. Yersinia adhesin A (YadA) from Yersinia enterocolitica is a prototypical TAA that is used extensively to study the structure and function of the type Vc secretion system. A solid‐state NMR study of the membrane anchor domain of YadA previously revealed a flexible stretch of small residues, termed the ASSA region, that links the membrane anchor to the stalk domain. In this study, we present evidence that single amino acid proline substitutions produce two different conformers of the membrane anchor domain of YadA; one with the N‐termini facing the extracellular surface, and a second with the N‐termini located in the periplasm. We propose that TAAs adopt a hairpin intermediate during secretion, as has been shown before for other subtypes of the type V secretion system. As the YadA transition state intermediate can be isolated from the outer membrane, future structural studies should be possible to further unravel details of the autotransport process.

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Section: Methodsmentioning

confidence: 99%

Insights into the autotransport process of a trimeric autotransporter, Yersinia Adhesin A (YadA)

Chauhan

Hatlem

Orwick‐Rydmark

et al. 2019

Molecular Microbiology

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“…The in vitro PGN pull‐down assay was adapted from Leo et al . (). In brief, 1 µM protein was incubated with 2 µl PGN (10 mg ml −1 ) from Anabaena sp.…”

Section: Methodsmentioning

confidence: 97%

LytM factor Alr3353 affects filament morphology and cell–cell communication in the multicellular cyanobacterium Anabaena sp. PCC 7120

Bornikoel

Staiger

Madlung

et al. 2018

Molecular Microbiology

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Heterocyst-forming cyanobacteria are organized as multicellular filaments of tightly interacting, functionally specialized cells. N -fixing heterocysts differentiate from vegetative cells under nitrogen limitation in a semi-regular pattern along the filament. Diazotrophic growth requires metabolite exchange between neighboring cells within the filament. This exchange occurs via cell-cell junction complexes that span the gap between the plasma membranes and thereby cross the septal peptidoglycan through an array of uniform nanopores formed by AmiC-type cell wall hydrolases. We investigated how the lytic hydrolase AmiC1 (Alr0092) from Anabaena sp. PCC 7120, whose activity needs to be tightly controlled to avoid cell lysis, is regulated by the LytM factor Alr3353. Inactivation of alr3353 resulted in significantly fewer nanopores and as a consequence, a lower rate of fluorescent tracer exchange between cells. The mutant was not able to grow with N as sole nitrogen source, although heterocysts were formed. Alr3353 localized mainly to fully developed intercellular septa of vegetative cells. The purified protein bound to peptidoglycan and enhanced the hydrolytic activity of AmiC1 in vitro. Our data show that the LytM factor Alr3353 regulates nanopore formation and cell-cell communication by directly interacting with AmiC1.

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“…Their modular passenger domains are composed of IgG-like and lectin-like domains. These proteins appear to also have periplasmic extensions involved in dimerization (Leo et al, 2015a). …”

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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The Intimin periplasmic domain mediates dimerisation and binding to peptidoglycan

Cited by 31 publications

References 52 publications

Insights into the autotransport process of a trimeric autotransporter, Yersinia Adhesin A (YadA)

Insights into the autotransport process of a trimeric autotransporter, Yersinia Adhesin A (YadA)

LytM factor Alr3353 affects filament morphology and cell–cell communication in the multicellular cyanobacterium Anabaena sp. PCC 7120

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

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