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      Weakly haemolytic variants of Brachyspira hyodysenteriae newly emerged in Europe belong to a distinct subclade with unique genetic properties

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          Abstract

          Brachyspira ( B.) hyodysenteriae is widespread globally, and can cause mucohaemorrhagic colitis (swine dysentery, SD) with severe economic impact in infected herds. Typical strains of B. hyodysenteriae are strongly haemolytic on blood agar, and the haemolytic activity is believed to contribute to virulence in vivo. However, recently there have been reports of atypical weakly haemolytic isolates of B. hyodysenteriae (whBh). In this study, 34 European whBh and 82 strongly haemolytic isolates were subjected to comparative genomic analysis. A phylogenetic tree constructed using core single nucleotide polymorphisms showed that the whBh formed a distinct sub-clade. All eight genes previously associated with haemolysis in B. hyodysenteriae were present in the whBh. No consistent patterns of amino acid substitutions for all whBh were found in these genes. In contrast, a genome region containing six coding sequences (CDSs) had consistent nucleotide sequence differences between strongly and whBh isolates. Two CDSs were predicted to encode ABC transporter proteins, and a TolC family protein, which may have a role in the export of haemolysins from B. hyodysenteriae. Another difference in this region was the presence of three CDSs in whBh that are pseudogenes in strongly haemolytic isolates. One of the intact CDSs from whBh encoded a predicted PadR-like transcriptional repressor that may play a role in repression of haemolysis functions. In summary, a sub-clade of whBh isolates has emerged in Europe, and several genomic differences, that potentially explain the weakly haemolytic phenotype, were identified. These markers may provide targets for discriminatory molecular tests needed in SD surveillance.

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          Most cited references42

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          The Type 1 secretion pathway - the hemolysin system and beyond.

          Type 1 secretion systems (T1SS) are wide-spread among Gram-negative bacteria. An important example is the secretion of the hemolytic toxin HlyA from uropathogenic strains. Secretion is achieved in a single step directly from the cytosol to the extracellular space. The translocation machinery is composed of three indispensable membrane proteins, two in the inner membrane, and the third in the outer membrane. The inner membrane proteins belong to the ABC transporter and membrane fusion protein families (MFPs), respectively, while the outer membrane component is a porin-like protein. Assembly of the three proteins is triggered by accumulation of the transport substrate (HlyA) in the cytoplasm, to form a continuous channel from the inner membrane, bridging the periplasm and finally to the exterior. Interestingly, the majority of substrates of T1SS contain all the information necessary for targeting the polypeptide to the translocation channel - a specific sequence at the extreme C-terminus. Here, we summarize our current knowledge of regulation, channel assembly, translocation of substrates, and in the case of the HlyA toxin, its interaction with host membranes. We try to provide a complete picture of structure function of the components of the translocation channel and their interaction with the substrate. Although we will place the emphasis on the paradigm of Type 1 secretion systems, the hemolysin A secretion machinery from E. coli, we also cover as completely as possible current knowledge of other examples of these fascinating translocation systems. This article is part of a Special Issue entitled: Protein trafficking and secretion in bacteria. Guest Editors: Anastassios Economou and Ross Dalbey. © 2013 Elsevier B.V. All rights reserved.
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            Colistin resistance in Salmonella and Escherichia coli isolates from a pig farm in Great Britain.

            The objective of this study was to characterize colistin-resistant bacteria isolated from pigs on a farm in Great Britain following identification of a plasmid-borne colistin resistance mechanism in Escherichia coli from China.
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              AcrA, AcrB, and TolC of Escherichia coli Form a Stable Intermembrane Multidrug Efflux Complex.

              Many transporters of Gram-negative bacteria involved in the extracellular secretion of proteins and the efflux of toxic molecules operate by forming intermembrane complexes. These complexes are proposed to span both inner and outer membranes and create a bridge across the periplasm. In this study, we analyzed interactions between the inner and outer membrane components of the tri-partite multidrug efflux pump AcrAB-TolC from Escherichia coli. We found that, once assembled, the intermembrane AcrAB-TolC complex is stable during the separation of the inner and outer membranes and subsequent purification. All three components of the complex co-purify when the affinity tag is attached to either of the proteins suggesting bi-partite interactions between AcrA, AcrB, and TolC. We show that antibiotics, the substrates of AcrAB-TolC, stabilize interactions within the complex. However, the formation of the AcrAB-TolC complex does not require an input of energy.
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                Author and article information

                Contributors
                Roderick.Card@apha.gsi.gov.uk
                T.La@murdoch.edu.au
                burrough@iastate.edu
                Richard.Ellis@apha.gsi.gov.uk
                javier.nunez@genomicsmed.ie
                Jill.Thomson@sac.co.uk
                Maxime.Mahu@UGent.be
                N.Phillips@murdoch.edu.au
                david.hampson@cityu.edu.hk
                Judith.Rohde@tiho-hannover.de
                awt1000@cam.ac.uk
                Journal
                Vet Res
                Vet. Res
                Veterinary Research
                BioMed Central (London )
                0928-4249
                1297-9716
                7 March 2019
                7 March 2019
                2019
                : 50
                : 21
                Affiliations
                [1 ]ISNI 0000 0004 1765 422X, GRID grid.422685.f, Department of Bacteriology, , Animal and Plant Health Agency, ; Addlestone, UK
                [2 ]ISNI 0000 0004 0436 6763, GRID grid.1025.6, School of Veterinary and Life Sciences, , Murdoch University, ; Perth, Australia
                [3 ]ISNI 0000 0004 1936 7312, GRID grid.34421.30, Veterinary Diagnostic Laboratory, , Iowa State University, ; Ames, USA
                [4 ]ISNI 0000 0004 1765 422X, GRID grid.422685.f, Surveillance and Laboratory Services Department, , Animal and Plant Health Agency, ; Addlestone, UK
                [5 ]ISNI 0000 0001 0170 6644, GRID grid.426884.4, Veterinary Services, , Scotland’s Rural College, ; Penicuik, UK
                [6 ]ISNI 0000 0001 2069 7798, GRID grid.5342.0, Department of Pathology, Bacteriology and Avian Diseases, Faculty of Veterinary Medicine, , Ghent University, ; Ghent, Belgium
                [7 ]ISNI 0000 0004 1792 6846, GRID grid.35030.35, Department of Infectious Diseases and Public Health, , City University of Hong Kong, ; Kowloon Tong, Hong Kong
                [8 ]ISNI 0000 0001 0126 6191, GRID grid.412970.9, Institute for Microbiology, , University of Veterinary Medicine, ; Hannover, Germany
                [9 ]ISNI 0000000121885934, GRID grid.5335.0, Department of Veterinary Medicine, , University of Cambridge, ; Cambridge, UK
                [10 ]GRID grid.496869.c, Present Address: Genomics Medicine Ireland, ; Dublin, Ireland
                Author information
                http://orcid.org/0000-0002-4671-2164
                Article
                639
                10.1186/s13567-019-0639-x
                6407217
                30845993
                ae4244e5-d448-4c6e-885b-04f3f2d1f5e1
                © The Author(s) 2019

                Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License ( http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The Creative Commons Public Domain Dedication waiver ( http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.

                History
                : 10 December 2018
                : 26 February 2019
                Funding
                Funded by: FundRef http://dx.doi.org/10.13039/501100000277, Department for Environment, Food and Rural Affairs;
                Funded by: PIC Deutschland
                Funded by: BHZP
                Categories
                Research Article
                Custom metadata
                © The Author(s) 2019

                Veterinary medicine
                Veterinary medicine

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