Data_Sheet_1_Flux, Impact, and Fate of Halogenated Xenobiotic Compounds in the Gut.XLSX

<p>Humans and their associated microbiomes are exposed to numerous xenobiotics through drugs, dietary components, personal care products as well as environmental chemicals. Most of the reciprocal interactions between the microbiota and xenobiotics, such as halogenated compounds, occur within the human gut harboring diverse and dense microbial communities. Here, we provide an overview of the flux of halogenated compounds in the environment, and diverse exposure routes of human microbiota to these compounds. Subsequently, we review the impact of halogenated compounds in perturbing the structure and function of gut microbiota and host cells. In turn, cultivation-dependent and metagenomic surveys of dehalogenating genes revealed the potential of the gut microbiota to chemically alter halogenated xenobiotics and impact their fate. Finally, we provide an outlook for future research to draw attention and attract interest to study the bidirectional impact of halogenated and other xenobiotic compounds and the gut microbiota.</p

Data_Sheet_2_Flux, Impact, and Fate of Halogenated Xenobiotic Compounds in the Gut.DOCX

<p>Humans and their associated microbiomes are exposed to numerous xenobiotics through drugs, dietary components, personal care products as well as environmental chemicals. Most of the reciprocal interactions between the microbiota and xenobiotics, such as halogenated compounds, occur within the human gut harboring diverse and dense microbial communities. Here, we provide an overview of the flux of halogenated compounds in the environment, and diverse exposure routes of human microbiota to these compounds. Subsequently, we review the impact of halogenated compounds in perturbing the structure and function of gut microbiota and host cells. In turn, cultivation-dependent and metagenomic surveys of dehalogenating genes revealed the potential of the gut microbiota to chemically alter halogenated xenobiotics and impact their fate. Finally, we provide an outlook for future research to draw attention and attract interest to study the bidirectional impact of halogenated and other xenobiotic compounds and the gut microbiota.</p

Metadata

Metadata for the 1172 samples in the HITChip data matrix including age, sex, geographic region, DNA extraction information, projectID, probe-level Shannon diversity, BMI group,subjectID and time point. For units and other details, see the README file

HITChip phylogenetic microarray data matrix

Profiling of 130 genus-like taxa across 1006 western subjects based on the Human Intestinal Tract (HIT)Chip phylogenetic microarray

Summary of pilus phenotypes observed in derivatives of <i>Lactococcus lactis</i> NZ9000, <i>Lactobacillus rhamnosus</i> GG and PB12.

<p>The AA replacement is shaded in light grey within the GYPSY motif (bold AA residues).</p

Western blotting analysis of <i>L</i>. <i>lactis</i> MG1363 PPiA KO mutant and its complemented mutant, where the SpaA-SrtC1 cassette was introduced.

<p>SpaA pilin proteins were detected using anti-SpaA polyclonal antibodies. Legend: #, protein weight marker; HMWL, high molecular weight ladder; *, band corresponding to elongated pilus structures.</p

Bacterial strains and plasmids used in the present study.

<p>Bacterial strains and plasmids used in the present study.</p

Electron microscopy observations of <i>L</i>. <i>lactis</i> NZ9000 producing various SpaA pilus structures.

<p>Bacterial cells were immunogold-labeled with anti-SpaA serum and gold particles (10 nm). Legend: A, NZ9000 + SpaA-SrtC1; B, NZ9000 + SpaA-SrtC1^{Y29G, P30G}; C, NZ9000 + SpaA-SrtC1^P30G; D, NZ9000 + SpaA-SrtC1^Y29G.</p

Modelling of the region containing the GYPSY motif of the <i>Lb</i>. <i>rhamnosus</i> GG SrtC1 with kinked proline residue.

<p>(A) Output prediction results using PSIPRED server [<a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0153373#pone.0153373.ref043" target="_blank">43</a>,<a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0153373#pone.0153373.ref044" target="_blank">44</a>] indicated that the GYPSY motif introduces a breakage within an α-helix as opposed to some mutant variants; (B) and (C), <i>ab initio</i> model of the GYPSY motif. The kinked proline residue is shaded in fuchsia. The relevant AA modification(s) introduced in the present study are shown in vivid green.</p

Western blotting analysis of <i>L</i>. <i>lactis</i> NZ9000 expressing different <i>spaA-srtC</i>1 gene variants, where the GYPSY motif has been altered by AA substitution.

<p><b>SpaA pilin proteins were detected using anti-SpaA polyclonal antibodies.</b> Legend: #, protein weight marker; HMWL, high molecular weight ladder; *, band corresponding to elongated pilus structures.</p