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Functional and Structural Characterization of the UDP-Glucose Dehydrogenase Involved in Capsular Polysaccharide Biosynthesis from Campylobacter jejuni

  • Alexander S. Riegert
    Alexander S. Riegert
    Department of Biochemistry & Biophysics, Texas A&M University, College Station, Texas 77843, United States
  •  and 
  • Frank M. Raushel*
    Frank M. Raushel
    Department of Biochemistry & Biophysics, Texas A&M University, College Station, Texas 77843, United States
    Department of Chemistry, Texas A&M University, College Station, Texas 77843, United States
    *Email: [email protected]
Cite this: Biochemistry 2021, 60, 9, 725–734
Publication Date (Web):February 23, 2021
https://doi.org/10.1021/acs.biochem.0c00953
Copyright © 2021 American Chemical Society

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    Abstract

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    Campylobacter jejuni is a pathogenic organism that can cause campylobacteriosis in children and adults. Most commonly, campylobacter infection is brought on by consumption of raw or undercooked poultry, unsanitary drinking water, or pet feces. Surrounding the C. jejuni bacterium is a coat of sugar molecules known as the capsular polysaccharide (CPS). The capsular polysaccharide can be very diverse among the different strains of C. jejuni, and this diversity is considered important for evading the host immune system. Modifications to the CPS of C. jejuni NCTC 11168 include O-methylation, phosphoramidylation, and amidation of glucuronate with either serinol or ethanolamine. The enzymes responsible for amidation of glucuronate are currently unknown. In this study, Cj1441, an enzyme expressed from the CPS biosynthetic gene cluster in C. jejuni NCTC 11168, was shown to catalyze the oxidation of UDP-α-d-glucose into UDP-α-d-glucuronic acid with NAD+ as the cofactor. No amide products were found in an attempt to determine whether the putative thioester intermediate formed during the oxidation of UDP-glucose by Cj1441 could be captured in the presence of added amines. The three-dimensional crystal structure of Cj1441 was determined in the presence of NAD+ and UDP-glucose bound in the active site of the enzyme (Protein Data Bank entry 7KWS). A more thorough bioinformatic analysis of the CPS gene cluster suggests that the amidation activity is localized to the t-terminal half of Cj1438, a bifunctional enzyme that is currently annotated as a sugar transferase.

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    The Supporting Information is available free of charge at https://pubs.acs.org/doi/10.1021/acs.biochem.0c00953.

    • Mass spectra of reaction products, structural comparison of Cj1441 with UDP-glucose 6-dehydrogenase from S. pyogenes, electron density for UDP-glucose in the active site of Cj1441, and sequence alignment between Cj1438 and WfdR from E. coli O143 (PDF)

    Accession Codes

    Cj1441, UniProt entry Q0PH3; PDB entry 7KWS.

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    Most electronic Supporting Information files are available without a subscription to ACS Web Editions. Such files may be downloaded by article for research use (if there is a public use license linked to the relevant article, that license may permit other uses). Permission may be obtained from ACS for other uses through requests via the RightsLink permission system: http://pubs.acs.org/page/copyright/permissions.html.

    Cited By

    This article is cited by 5 publications.

    1. Manas K. Ghosh, Frank M. Raushel. Biosynthesis of UDP-α-N-Acetyl-d-mannosaminuronic Acid and CMP-β-N-Acetyl-d-neuraminic Acid for the Capsular Polysaccharides of Campylobacter jejuni. Biochemistry 2024, 63 (5) , 688-698. https://doi.org/10.1021/acs.biochem.3c00664
    2. Alexander S. Riegert, Tamari Narindoshvili, Nicole E. Platzer, Frank M. Raushel. Functional Characterization of a HAD Phosphatase Involved in Capsular Polysaccharide Biosynthesis in Campylobacter jejuni. Biochemistry 2022, 61 (21) , 2431-2440. https://doi.org/10.1021/acs.biochem.2c00484
    3. Alexander S. Riegert, Tamari Narindoshvili, Frank M. Raushel. Discovery and Functional Characterization of a Clandestine ATP-Dependent Amidoligase in the Biosynthesis of the Capsular Polysaccharide from Campylobacter jejuni. Biochemistry 2022, 61 (2) , 117-124. https://doi.org/10.1021/acs.biochem.1c00707
    4. Alexander S. Riegert, Tamari Narindoshvili, Adriana Coricello, Nigel G. J. Richards, Frank M. Raushel. Functional Characterization of Two PLP-Dependent Enzymes Involved in Capsular Polysaccharide Biosynthesis from Campylobacter jejuni. Biochemistry 2021, 60 (37) , 2836-2843. https://doi.org/10.1021/acs.biochem.1c00439
    5. Hamed Rezayatmand, Nafiseh Golestani, Adele Sadat Haghighat Hoseini, Elaheh Mousavialmaleki, Mahsa Alem, Donya Farzane Yegane. Gene expression profile of Campylobacter jejuni in response to macrolide antibiotics. Archives of Microbiology 2024, 206 (3) https://doi.org/10.1007/s00203-024-03849-0

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