Fusarium virguliforme Transcriptional Plasticity Is Revealed by Host Colonization of Maize versus Soybean

Bacterial communities colonize epithelial surfaces of most animals. Several factors, including the innate immune system, mucus composition, and diet, have been identified as determinants of host-associated bacterial communities. Here we show that the early branching metazoan Hydra is able to modify bacterial quorum-sensing signals. We identified a eukaryotic mechanism that enables Hydra to specifically modify long-chain 3-oxo-homoserine lactones into their 3-hydroxy-HSL counterparts. Expression data revealed that Hydra’s main bacterial colonizer, Curvibacter sp., responds differentially to N-(3-hydroxydodecanoyl)-l-homoserine lactone (3OHC12-HSL) and N-(3-oxododecanoyl)-l-homoserine lactone (3OC12-HSL). Investigating the impacts of the different N-acyl-HSLs on host colonization elucidated that 3OHC12-HSL allows and 3OC12-HSL represses host colonization of Curvibacter sp. These results show that an animal manipulates bacterial quorum-sensing signals and that this modification leads to a phenotypic switch in the bacterial colonizers. This mechanism may enable the host to manipulate the gene expression and thereby the behavior of its bacterial colonizers.

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A highly efficient Agrobacterium tumefaciens-mediated transformation system for the postharvest pathogen Penicillium digitatum using DsRed and GFP to visualize citrus host colonization

Journal of Microbiological Methods ◽

10.1016/j.mimet.2017.11.019 ◽

2018 ◽

Vol 144 ◽

pp. 134-144 ◽

Cited By ~ 8

Author(s):

Tao Xuan Vu ◽

Tho Tien Ngo ◽

Linh Thi Dam Mai ◽

Tri-Thuc Bui ◽

Diep Hong Le ◽

...

Keyword(s):

Agrobacterium Tumefaciens ◽

Penicillium Digitatum ◽

Transformation System ◽

Host Colonization ◽

Highly Efficient

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Proteomic Profiling and the Predicted Interactome of Host Proteins in Compatible and Incompatible Interactions Between Soybean and Fusarium virguliforme

Applied Biochemistry and Biotechnology ◽

10.1007/s12010-016-2194-5 ◽

2016 ◽

Vol 180 (8) ◽

pp. 1657-1674 ◽

Cited By ~ 3

Author(s):

M. Javed Iqbal ◽

Maryam Majeed ◽

Maheen Humayun ◽

David A. Lightfoot ◽

Ahmed J. Afzal

Keyword(s):

Proteomic Profiling ◽

Host Proteins ◽

Fusarium Virguliforme ◽

Incompatible Interactions

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Pseudomonas aeruginosa PA14 biofilms produce R-bodies, extendable protein polymers with roles in host colonization and virulence

10.1101/2020.10.26.356394 ◽

2020 ◽

Author(s):

Bryan Wang ◽

Yu-Cheng Lin ◽

Jeanyoung Jo ◽

Alexa Price-Whelan ◽

Shujuan Tao McDonald ◽

...

Keyword(s):

Gene Expression ◽

Pseudomonas Aeruginosa ◽

Host Colonization ◽

Biofilm Growth ◽

Protein Polymers ◽

Virulent Strains

reb genes code for R-bodies: large, extendable polymers that are known for their roles in obligate endosymbioses. In the non-endosymbiotic pathogen Pseudomonas aeruginosa, reb homologues are part of a cluster found in virulent strains. Here, we demonstrate that R-bodies are produced in abundance by P. aeruginosa PA14 subpopulations during biofilm growth, identify regulators of reb gene expression, and show that reb genes are required for full colonization and virulence in host models.

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A Combination of Structural, Genetic, Phenotypic and Enzymatic Analyses Reveals the Importance of a Predicted Fucosyltransferase to Protein O-Glycosylation in the Bacteroidetes

Biomolecules ◽

10.3390/biom11121795 ◽

2021 ◽

Vol 11 (12) ◽

pp. 1795

Author(s):

Markus B. Tomek ◽

Bettina Janesch ◽

Matthias L. Braun ◽

Manfred Taschner ◽

Rudolf Figl ◽

...

Keyword(s):

Structural Analysis ◽

Mutational Analysis ◽

Bacteroides Fragilis ◽

Host Colonization ◽

Acceptor Specificity ◽

Hexose Sugars ◽

Full Structure ◽

Bacteroidetes Phylum ◽

General Protein

Diverse members of the Bacteroidetes phylum have general protein O-glycosylation systems that are essential for processes such as host colonization and pathogenesis. Here, we analyzed the function of a putative fucosyltransferase (FucT) family that is widely encoded in Bacteroidetes protein O-glycosylation genetic loci. We studied the FucT orthologs of three Bacteroidetes species—Tannerella forsythia, Bacteroides fragilis, and Pedobacter heparinus. To identify the linkage created by the FucT of B. fragilis, we elucidated the full structure of its nine-sugar O-glycan and found that l-fucose is linked β1,4 to glucose. Of the two fucose residues in the T. forsythia O-glycan, the fucose linked to the reducing-end galactose was shown by mutational analysis to be l-fucose. Despite the transfer of l-fucose to distinct hexose sugars in the B. fragilis and T. forsythia O-glycans, the FucT orthologs from B. fragilis, T. forsythia, and P. heparinus each cross-complement the B. fragilis ΔBF4306 and T. forsythia ΔTanf_01305 FucT mutants. In vitro enzymatic analyses showed relaxed acceptor specificity of the three enzymes, transferring l-fucose to various pNP-α-hexoses. Further, glycan structural analysis together with fucosidase assays indicated that the T. forsythia FucT links l-fucose α1,6 to galactose. Given the biological importance of fucosylated carbohydrates, these FucTs are promising candidates for synthetic glycobiology.

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Role of Campylobacter jejuni Respiratory Oxidases and Reductases in Host Colonization

Applied and Environmental Microbiology ◽

10.1128/aem.02261-07 ◽

2008 ◽

Vol 74 (5) ◽

pp. 1367-1375 ◽

Cited By ~ 66

Author(s):

Rebecca A. Weingarten ◽

Jesse L. Grimes ◽

Jonathan W. Olson

Keyword(s):

Campylobacter Jejuni ◽

Anaerobic Respiration ◽

Wild Type ◽

Respiratory Enzymes ◽

Host Colonization ◽

Enzymatic Function ◽

Food Borne ◽

Transport Chain ◽

Respiratory Oxidases

ABSTRACT Campylobacter jejuni is the leading cause of human food-borne bacterial gastroenteritis. The C. jejuni genome sequence predicts a branched electron transport chain capable of utilizing multiple electron acceptors. Mutants were constructed by disrupting the coding regions of the respiratory enzymes nitrate reductase (napA::Cm), nitrite reductase (nrfA::Cm), dimethyl sulfoxide, and trimethylamine N-oxide reductase (termed Cj0264::Cm) and the two terminal oxidases, a cyanide-insensitive oxidase (cydA::Cm) and cbb3-type oxidase (ccoN::Cm). Each strain was characterized for the loss of the associated enzymatic function in vitro. The strains were then inoculated into 1-week-old chicks, and the cecal contents were assayed for the presence of C. jejuni 2 weeks postinoculation. cydA::Cm and Cj0264c::Cm strains colonized as well as the wild type; napA::Cm and nrfA::Cm strains colonized at levels significantly lower than the wild type. The ccoN::Cm strain was unable to colonize the chicken; no colonies were recovered at the end of the experiment. While there appears to be a role for anaerobic respiration in host colonization, oxygen is the most important respiratory acceptor for C. jejuni in the chicken cecum.

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