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      Complete genome sequence of N 2-fixing model strain Klebsiella sp. nov. M5al, which produces plant cell wall-degrading enzymes and siderophores

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          Highlights

          • •

            Complete genome of the model N 2-fixing and 1,3-propanediol-producing strain M5al is presented.

          • •

            Strain M5al belongs to a novel species closely related to Klebsiella michiganensis.

          • •

            Strain M5al produces and secretes plant cell wall-degrading enzymes.

          • •

            Strain M5al is not pathogenic to plants and colonizes roots like a rhizobacterium.

          • •

            Strain M5al contains the gene cluster for synthesis and transport of yersiniabactin.

          Abstract

          The bacterial strain M5al is a model strain for studying the molecular genetics of N 2-fixation and molecular engineering of microbial production of platform chemicals 1,3-propanediol and 2,3-butanediol. Here, we present the complete genome sequence of the strain M5al, which belongs to a novel species closely related to Klebsiella michiganensis. M5al secretes plant cell wall-degrading enzymes and colonizes rice roots but does not cause soft rot disease. M5al also produces siderophores and contains the gene clusters for synthesis and transport of yersiniabactin which is a critical virulence factor for Klebsiella pathogens in causing human disease. We propose that the model strain M5al can be genetically modified to study bacterial N 2-fixation in association with non-legume plants and production of 1,3-propanediol and 2,3-butanediol through degradation of plant cell wall biomass.

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          Diverging roles of bacterial siderophores during infection.

          Victoria I. Holden, Michael Bachman (2015)
          Siderophores are low molecular weight, high affinity iron chelating molecules that are essential virulence factors in many Gram-negative bacterial pathogens. Whereas the chemical structure of siderophores is extremely variable, the function of siderophores has been narrowly defined as the chelation and delivery of iron to bacteria for proliferation. The discovery of the host protein Lipocalin 2, capable of specifically sequestering the siderophore Enterobactin but not its glycosylated-derivative Salmochelin, indicated that diversity in structure could be an immune evasion mechanism that provides functional redundancy during infection. However, there is growing evidence that siderophores are specialized in their iron-acquisition functions, can perturb iron homeostasis in their hosts, and even bind non-iron metals to promote bacterial fitness. The combination of siderophores produced by a pathogen can enable inter-bacterial competition, modulate host cellular pathways, and determine the bacterial "replicative niche" during infection. This review will examine both classical and novel functions of siderophores to address the concept that siderophores are non-redundant virulence factors used to enhance bacterial pathogenesis.
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            The role of secretion systems and small molecules in soft-rot Enterobacteriaceae pathogenicity.

            Pablo Rodríguez-Gonzálvez, Emilia López-Solanilla, Iris Yedidia … (2011)
            Soft-rot Enterobacteriaceae (SRE), which belong to the genera Pectobacterium and Dickeya, consist mainly of broad host-range pathogens that cause wilt, rot, and blackleg diseases on a wide range of plants. They are found in plants, insects, soil, and water in agricultural regions worldwide. SRE encode all six known protein secretion systems present in gram-negative bacteria, and these systems are involved in attacking host plants and competing bacteria. They also produce and detect multiple types of small molecules to coordinate pathogenesis, modify the plant environment, attack competing microbes, and perhaps to attract insect vectors. This review integrates new information about the role protein secretion and detection and production of ions and small molecules play in soft-rot pathogenicity.
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              Klebsiella pneumoniae Siderophores Induce Inflammation, Bacterial Dissemination, and HIF-1α Stabilization during Pneumonia

              Victoria I. Holden, Paul Breen, Sébastien Houle … (2016)
              ABSTRACT Klebsiella pneumoniae is a Gram-negative pathogen responsible for a wide range of infections, including pneumonia and bacteremia, and is rapidly acquiring antibiotic resistance. K. pneumoniae requires secretion of siderophores, low-molecular-weight, high-affinity iron chelators, for bacterial replication and full virulence. The specific combination of siderophores secreted by K. pneumoniae during infection can impact tissue localization, systemic dissemination, and host survival. However, the effect of these potent iron chelators on the host during infection is unknown. In vitro, siderophores deplete epithelial cell iron, induce cytokine secretion, and activate the master transcription factor hypoxia inducible factor-1α (HIF-1α) protein that controls vascular permeability and inflammatory gene expression. Therefore, we hypothesized that siderophore secretion by K. pneumoniae directly contributes to inflammation and bacterial dissemination during pneumonia. To examine the effects of siderophore secretion independently of bacterial growth, we performed infections with tonB mutants that persist in vivo but are deficient in siderophore import. Using a murine model of pneumonia, we found that siderophore secretion by K. pneumoniae induces the secretion of interleukin-6 (IL-6), CXCL1, and CXCL2, as well as bacterial dissemination to the spleen, compared to siderophore-negative mutants at an equivalent bacterial number. Furthermore, we determined that siderophore-secreting K. pneumoniae stabilized HIF-1α in vivo and that bacterial dissemination to the spleen required alveolar epithelial HIF-1α. Our results indicate that siderophores act directly on the host to induce inflammatory cytokines and bacterial dissemination and that HIF-1α is a susceptibility factor for bacterial invasion during pneumonia.
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                Author and article information

                Contributors
                Qianli An
                Journal
                Journal ID (nlm-ta): Biotechnol Rep (Amst)
                Journal ID (iso-abbrev): Biotechnol Rep (Amst)
                Title: Biotechnology Reports
                Publisher: Elsevier
                ISSN (Electronic): 2215-017X
                Publication date PMC-release: 22 November 2017
                Publication date Collection: March 2018
                Publication date (Electronic): 22 November 2017
                Volume: 17
                Pages: 6-9
                Affiliations
                [a ]Ministry of Agriculture Key Lab of Molecular Biology of Crop Pathogens and Insects, Institute of Biotechnology, Zhejiang University, Hangzhou 310058, China
                [b ]YK Pao School, Shanghai 201620, China
                Author notes
                [* ]Corresponding author. an@ 123456zju.edu.cn
                [1]

                Present address: Department of Biochemistry and Molecular Biology, Baylor College of Medicine, One Baylor Plaza, Houston, TX 77030, USA.

                Article
                Publisher ID: S2215-017X(17)30262-X
                DOI: 10.1016/j.btre.2017.11.006
                PMC ID: 5723360
                PubMed ID: 29234606
                SO-VID: 4c5f07b1-e52a-4b95-b4f4-7936d42b810d
                Copyright © © 2017 The Authors
                License:

                This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).

                History
                Date received : 17 September 2017
                Date revision received : 17 November 2017
                Date accepted : 21 November 2017
                Categories
                Subject: Article

                Keywords: klebsiella oxytoca,klebsiella michiganensis,nitrogen fixation,carbohydrate-active enzyme,type ii secretion system
                Data availability:
                Keywords: klebsiella oxytoca, klebsiella michiganensis, nitrogen fixation, carbohydrate-active enzyme, type ii secretion system

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