c concisus genomes atcc 33237  (ATCC)

Journal: Biochemistry

Article Title: Characterization of PglJ, a Glycosyltransferase in the Campylobacter concisus N-linked Protein Glycosylation Pathway that Expands Glycan Diversity

doi: 10.1021/acs.biochem.3c00564

Figure Lengend Snippet: A) The protein glycosylation (pgl) pathways in C. jejuni and C. concisus, B) pgl loci, C) the diverse, isolated N-linked glycans from different Campylobacter bacteria14 and D) the possible UDP-HexNAcA sugar donors for the PglJ glycosyltransferase.

Article Snippet: Measurements were carried out in triplicate for C. concisus ATCC 33237/13826 strain PglJ, and in duplicate for C. jejuni PglJ.

Techniques: Glycoproteomics, Isolation

Journal: Biochemistry

Article Title: Characterization of PglJ, a Glycosyltransferase in the Campylobacter concisus N-linked Protein Glycosylation Pathway that Expands Glycan Diversity

doi: 10.1021/acs.biochem.3c00564

Figure Lengend Snippet: A) UDP-sugar substrate screen with PglJs from C. concisus and C. jejuni. Error bars are given for mean ± SEM, n = 2. B) Single enzyme kinetic parameters. Confidence intervals (95%) and parameters were calculated using nonlinear regression (curve fit, Michaelis-Mention) using GraphPad Prism 8, n = 2–3.

Article Snippet: Measurements were carried out in triplicate for C. concisus ATCC 33237/13826 strain PglJ, and in duplicate for C. jejuni PglJ.

Techniques:

Journal: Biochemistry

Article Title: Characterization of PglJ, a Glycosyltransferase in the Campylobacter concisus N-linked Protein Glycosylation Pathway that Expands Glycan Diversity

doi: 10.1021/acs.biochem.3c00564

Figure Lengend Snippet: A) Displayed are PglJ sequence alignments. PglJs above the black line prefer GalNAcA according to established literature, while those below react with non-GalNAcA substrates. Our study determined that C. concisus PglJ 13826 has a preference for GalNAcA, suggesting it belongs to the group delineated by the red line. B) Glycosyltransferase activity assays containing a UDP-sugar substrate screen with varying concentrations of C. concisus 33237 S120N/R122C PglJ. Error bars are given for mean ± SEM, n = 2.

Article Snippet: Measurements were carried out in triplicate for C. concisus ATCC 33237/13826 strain PglJ, and in duplicate for C. jejuni PglJ.

Techniques: Sequencing, Activity Assay

Journal: Biochemistry

Article Title: Characterization of PglJ, a Glycosyltransferase in the Campylobacter concisus N-linked Protein Glycosylation Pathway that Expands Glycan Diversity

doi: 10.1021/acs.biochem.3c00564

Figure Lengend Snippet: An HPLC-based assay to validate the activity of the dehydrogenase from C. concisus strain 13826. Lanes: A) UDP-GalNAc reaction, B) UDP-GlcNAc reaction, C) UDP-GlcNAc standard, D) UDP-GalNAc standard, E) UDP-GalNAcA standard, F) UDP-GlcNAcA standard, and G) NADH standard. The supporting information contains full HPLC traces.

Article Snippet: Measurements were carried out in triplicate for C. concisus ATCC 33237/13826 strain PglJ, and in duplicate for C. jejuni PglJ.

Techniques: Activity Assay

Journal: Biochemistry

Article Title: Characterization of PglJ, a Glycosyltransferase in the Campylobacter concisus N-linked Protein Glycosylation Pathway that Expands Glycan Diversity

doi: 10.1021/acs.biochem.3c00564

Figure Lengend Snippet: The proposed N-linked protein glycosylation pathway in C. concisus strain 33237.

Article Snippet: Measurements were carried out in triplicate for C. concisus ATCC 33237/13826 strain PglJ, and in duplicate for C. jejuni PglJ.

Techniques: Glycoproteomics