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<t>(A-E)</t> <t>SDS-PAGE</t> of purified LPS stained with ProQ Emerald 300 kit. Higher mobility LPS denoted ($). (A) Previously described H. pylori mouse-adapted strains and their parent human isolate. (B-E) PMSS1, SS1, and mouse outputs of PMSS1 at indicated times post-infection in C57BL6/N (black) or GIM mice (red). (F) Predicted amino acid variants of the α-( , )-fucosyltransferase FutB, the putative galactosyltransferase HPYLPMSS1_0826, G27 FutC (HpG27_0086), and the HpG27_579/580 loci from the subset of strains we sequenced. Strains and isolates are indicated next to the allele they are predicted to encode based on WGS.
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(A-E) SDS-PAGE of purified LPS stained with ProQ Emerald 300 kit. Higher mobility LPS denoted ($). (A) Previously described H. pylori mouse-adapted strains and their parent human isolate. (B-E) PMSS1, SS1, and mouse outputs of PMSS1 at indicated times post-infection in C57BL6/N (black) or GIM mice (red). (F) Predicted amino acid variants of the α-( , )-fucosyltransferase FutB, the putative galactosyltransferase HPYLPMSS1_0826, G27 FutC (HpG27_0086), and the HpG27_579/580 loci from the subset of strains we sequenced. Strains and isolates are indicated next to the allele they are predicted to encode based on WGS.

Journal: bioRxiv

Article Title: Helicobacter pylori allelic variation in cell surface genes influences human exoproteome binding and stomach tissue adherence

doi: 10.64898/2026.03.06.710112

Figure Lengend Snippet: (A-E) SDS-PAGE of purified LPS stained with ProQ Emerald 300 kit. Higher mobility LPS denoted ($). (A) Previously described H. pylori mouse-adapted strains and their parent human isolate. (B-E) PMSS1, SS1, and mouse outputs of PMSS1 at indicated times post-infection in C57BL6/N (black) or GIM mice (red). (F) Predicted amino acid variants of the α-( , )-fucosyltransferase FutB, the putative galactosyltransferase HPYLPMSS1_0826, G27 FutC (HpG27_0086), and the HpG27_579/580 loci from the subset of strains we sequenced. Strains and isolates are indicated next to the allele they are predicted to encode based on WGS.

Article Snippet: Samples were then run on 4-15% gradient SDS-PAGE Tris-glycine gels (Bio Rad Mini-PROTEAN TGX) with discontinuous running buffer (cathode: 0.1 M Tris, 0.1 M glycine, 0.1% SDS, pH 8.25; anode: 0.2 M Tris-HCl, pH 8.9) at 100 V until the dye front was near the bottom.

Techniques: SDS Page, Purification, Staining, Infection

(A) SDS-PAGE of purified LPS from a panel of deletions subset of the characterized G27 glycosyltransferases. Loss of O-antigen production was identified in wecA, wzk, HpG27_1046, HpG27_0437, HpG27_0094, and HpG27_1235 deletions. (B) Schematic of the G27 LPS structure with enzymes responsible for the addition of each unit, adapted from Li et al. . (C) Adherence of fluorescein-labeled H. pylori to FFPE GIM mouse stomach tissue. Number of adhered bacteria per area of tissue plotted in GraphPad Prism. Purple - values greater than one standard deviation above wild type average (dotted line), green - values one standard deviation below. Sequential tissue slices from the same animal graphed with the same symbol.

Journal: bioRxiv

Article Title: Helicobacter pylori allelic variation in cell surface genes influences human exoproteome binding and stomach tissue adherence

doi: 10.64898/2026.03.06.710112

Figure Lengend Snippet: (A) SDS-PAGE of purified LPS from a panel of deletions subset of the characterized G27 glycosyltransferases. Loss of O-antigen production was identified in wecA, wzk, HpG27_1046, HpG27_0437, HpG27_0094, and HpG27_1235 deletions. (B) Schematic of the G27 LPS structure with enzymes responsible for the addition of each unit, adapted from Li et al. . (C) Adherence of fluorescein-labeled H. pylori to FFPE GIM mouse stomach tissue. Number of adhered bacteria per area of tissue plotted in GraphPad Prism. Purple - values greater than one standard deviation above wild type average (dotted line), green - values one standard deviation below. Sequential tissue slices from the same animal graphed with the same symbol.

Article Snippet: Samples were then run on 4-15% gradient SDS-PAGE Tris-glycine gels (Bio Rad Mini-PROTEAN TGX) with discontinuous running buffer (cathode: 0.1 M Tris, 0.1 M glycine, 0.1% SDS, pH 8.25; anode: 0.2 M Tris-HCl, pH 8.9) at 100 V until the dye front was near the bottom.

Techniques: SDS Page, Purification, Labeling, Bacteria, Standard Deviation