scholarly journals Mechanism of interaction of an endofungal bacterium Serratia marcescens D1 with its host and non-host fungi

2019 ◽  
Author(s):  
Dibya Jyoti Hazarika ◽  
Trishnamoni Gautom ◽  
Assma Parveen ◽  
Gunajit Goswami ◽  
Madhumita Barooah ◽  
...  
Keyword(s):  
Serratia Marcescens ◽  
Type Vi Secretion System ◽  
Major Area ◽  
Fungal Cell ◽  
Type Vi Secretion ◽  
Mucor Irregularis ◽  
Fungal Hyphae ◽  
Genes Encoding ◽  
Mechanism Of Interaction

AbstractAssociation of bacteria with fungi is a major area of research in infection biology, however, very few strains of bacteria have been reported that can invade and reside within fungal hyphae. Here, we report the characterization of an endofungal bacterium Serratia marcescens D1 from Mucor irregularis SS7 hyphae. Upon re-inoculation, colonization of the endobacterium S. marcescens D1 in the hyphae of Mucor irregularis SS7 was demonstrated using stereo microscopy. However, S. marcescens D1 failed to invade into the hyphae of the tested Ascomycetes (except Fusarium oxysporum) and Basidiomycetes. Remarkably, Serratia marcescens D1 could invade and spread over the culture of F. oxysporum that resulted in mycelial death. Prodigiosin, the red pigment produced by the Serratia marcescens D1, helps the bacterium to invade fungal hyphae as revealed by the increasing permeability in fungal cell membrane. On the other hand, genes encoding the type VI secretion system (T6SS) assembly protein TssJ and an outer membrane associated murein lipoprotein also showed significant up-regulation during the interaction process, suggesting the involvement of T6SS in the invasion process.

scholarly journals AT6SS trans-kingdom effector is required for the delivery of a novel antibacterial toxin in Pseudomonas aeruginosa

2019 ◽  
Author(s):  
Benjamin Berni ◽  
Chantal Soscia ◽  
Djermoun Sarah ◽  
Ize Bérengère ◽  
Sophie Bleves
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Surrounding Medium ◽  
Host Cells ◽  
List Type ◽  
Type Vi Secretion System ◽  
Multiple Strategies ◽  
Type Vi Secretion ◽  
Host Infection ◽  
Opportunist Pathogen

AbstractPseudomonas aeruginosa has evolved multiple strategies to disarm and take advantage of its host. For this purpose this opportunist pathogen has particularly developed protein secretion in the surrounding medium or injection into host cells. Among this, the Type VI Secretion System (T6SS) is utilized to deliver effectors into eukaryotic host as well as target bacteria. It assembles into a contractile bacteriophage tail-like structure that functions like a crossbow, injecting an arrow loaded with effectors into the target cell. The repertoire of T6SS antibacterial effectors of P. aeruginosa is remarkably broad to promote environmental adaptation and survival in various bacterial communities, and presumably in the eukaryotic host too.Here we report the discovery a novel pair of antibacterial effector and immunity of P. aeruginosa, Tle3 and Tli3. Tli3 neutralizes the toxicity of Tle3 in the periplasm to protect from fratricide intoxication. The characterization of the secretion mechanism of Tle3 indicates that it requires a cytoplasmic adaptor, Tla3, to be targeted and loaded onto the VgrG2b spike and thus delivered by the H2-T6SS machinery. Tla3 is different from the other adaptors discovered so far, and defines a novel family among T6SS.Interestingly this led us to discover that VgrG2b that we previously characterized as an anti-eukaryotic effector possesses an antibacterial activity as well, as it is toxic towards Escherichia coli. VgrG2b is thus a novel trans-kingdom effector targeting both bacteria and eukaryotes. VgrG2b represents an interesting target for fighting against P. aeruginosa in the environment and in the context of host infection.HighlightsTle3 and Tli3 are a novel pair of antibacterial toxin and immunity of P. aeruginosaTla3 recruits Tle3 in the cytoplasm, and targets it to VgrG2bVgrG2b is required for Tle3 delivery into target bacteria by the H2-T6SSTla3 defines a novel type of T6SS adaptor with a DUF2875VgrG2b is a new trans-kingdom effector targeting both bacteria and eukaryotes

scholarly journals A family of Type VI secretion system effector proteins that form ion-selective pores

2019 ◽  
Vol 10 (1) ◽  
Author(s):  
Giuseppina Mariano ◽  
Katharina Trunk ◽  
David J. Williams ◽  
Laura Monlezun ◽  
Henrik Strahl ◽  
...  
Keyword(s):  
Opportunistic Pathogen ◽  
Effector Proteins ◽  
Type Vi Secretion System ◽  
Secretion Systems ◽  
New Family ◽  
Type Vi Secretion ◽  
Genes Encoding ◽  
Outer Membrane Permeability ◽  
Bacterial Effectors

AbstractType VI secretion systems (T6SSs) are nanomachines widely used by bacteria to deliver toxic effector proteins directly into neighbouring cells. However, the modes of action of many effectors remain unknown. Here we report that Ssp6, an anti-bacterial effector delivered by a T6SS of the opportunistic pathogen Serratia marcescens, is a toxin that forms ion-selective pores. Ssp6 inhibits bacterial growth by causing depolarisation of the inner membrane in intoxicated cells, together with increased outer membrane permeability. Reconstruction of Ssp6 activity in vitro demonstrates that it forms cation-selective pores. A survey of bacterial genomes reveals that genes encoding Ssp6-like effectors are widespread in Enterobacteriaceae and often linked with T6SS genes. We conclude that Ssp6 and similar proteins represent a new family of T6SS-delivered anti-bacterial effectors.

scholarly journals A Conserved α-Helix Essential for a Type VI Secretion-Like System of Francisella tularensis

2009 ◽  
Vol 191 (8) ◽  
pp. 2431-2446 ◽  
Author(s):  
Jeanette E. Bröms ◽  
Moa Lavander ◽  
Anders Sjöstedt
Keyword(s):  
Complex Formation ◽  
Francisella Tularensis ◽  
Yersinia Pseudotuberculosis ◽  
Point Mutations ◽  
Human Pathogens ◽  
Type Vi Secretion System ◽  
Type Vi Secretion ◽  
Serovar Typhimurium ◽  
Genes Encoding ◽  
Α Helix

ABSTRACT Francisella tularensis harbors genes with similarity to genes encoding components of a type VI secretion system (T6SS) recently identified in several gram-negative bacteria. These genes include iglA and iglB encoding IglA and IglB, homologues of which are conserved in most T6SSs. We used a yeast two-hybrid system to study the interaction of the Igl proteins of F. tularensis LVS. We identified a region of IglA, encompassing residues 33 to 132, necessary for efficient binding to IglB, as well as for IglAB protein stability and intramacrophage growth. In particular, residues 103 to 122, overlapping a highly conserved α-helix, played an absolutely essential role. Point mutations within this domain caused modest defects in IglA-IglB binding in the yeast Saccharomyces cerevisiae but markedly impaired intramacrophage replication and phagosomal escape, resulting in severe attenuation of LVS in mice. Thus, IglA-IglB complex formation is clearly crucial for Francisella pathogenicity. This interaction may be universal to type VI secretion, since IglAB homologues of Yersinia pseudotuberculosis, Pseudomonas aeruginosa, Vibrio cholerae, Salmonella enterica serovar Typhimurium, and Escherichia coli were also shown to interact in yeast, and the interaction was dependent on preservation of the same α-helix. Heterologous interactions between nonnative IglAB proteins further supported the notion of a conserved binding site. Thus, IglA-IglB complex formation is clearly crucial for Francisella pathogenicity, and the same interaction is conserved in other human pathogens.

scholarly journals The Francisella Pathogenicity Island Protein PdpD Is Required for Full Virulence and Associates with Homologues of the Type VI Secretion System

2008 ◽  
Vol 190 (13) ◽  
pp. 4584-4595 ◽  
Author(s):  
Jagjit S. Ludu ◽  
Olle M. de Bruin ◽  
Barry N. Duplantis ◽  
Crystal L. Schmerk ◽  
Alicia Y. Chou ◽  
...  
Keyword(s):  
North America ◽  
Outer Membrane ◽  
Bacterial Pathogen ◽  
Pathogenicity Island ◽  
Secretion System ◽  
Type Vi Secretion System ◽  
Secretion Systems ◽  
Intracellular Growth ◽  
Type Vi Secretion ◽  
Genes Encoding

ABSTRACT Francisella tularensis is a highly infectious, facultative intracellular bacterial pathogen that is the causative agent of tularemia. Nearly a century ago, researchers observed that tularemia was often fatal in North America but almost never fatal in Europe and Asia. The chromosomes of F. tularensis strains carry two identical copies of the Francisella pathogenicity island (FPI), and the FPIs of North America-specific biotypes contain two genes, anmK and pdpD, that are not found in biotypes that are distributed over the entire Northern Hemisphere. In this work, we studied the contribution of anmK and pdpD to virulence by using F. novicida, which is very closely related to F. tularensis but which carries only one copy of the FPI. We showed that anmK and pdpD are necessary for full virulence but not for intracellular growth. This is in sharp contrast to most other FPI genes that have been studied to date, which are required for intracellular growth. We also showed that PdpD is localized to the outer membrane. Further, overexpression of PdpD affects the cellular distribution of FPI-encoded proteins IglA, IglB, and IglC. Finally, deletions of FPI genes encoding proteins that are homologues of known components of type VI secretion systems abolished the altered distribution of IglC and the outer membrane localization of PdpD.

scholarly journals Isolation and characterization of genes encoding two chitinase enzymes from Serratia marcescens

1986 ◽  
Vol 5 (3) ◽  
pp. 467-473 ◽  
Author(s):  
Jonathan D.G. Jones ◽  
Karen L. Grady ◽  
Trevor V. Suslow ◽  
John R. Bedbrook
Keyword(s):  
Serratia Marcescens ◽  
Isolation And Characterization ◽  
Genes Encoding
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