Academic Journal
Functional analysis of the Helicobacter pullorum N-linked protein glycosylation system
| العنوان: | Functional analysis of the Helicobacter pullorum N-linked protein glycosylation system |
|---|---|
| المؤلفون: | Adrian J Jervis, Amanda Wood, Joel A Cain, Jonathan A Butler, Helen Frost, Elizabeth Lord, Rebecca Langdon, Stuart J Cordwell, Brendan W Wren, Dennis Linton |
| سنة النشر: | 2018 |
| مصطلحات موضوعية: | Biological sciences, Biochemistry and cell biology, Genetics, Biomedical and clinical sciences, ACTINOBACILLUS-PLEUROPNEUMONIAE, ARCHAEA, bacteria, BACTERIAL OLIGOSACCHARYLTRANSFERASE, Biochemistry & Molecular Biology, BIOSYNTHESIS, CAMPYLOBACTER-JEJUNI, CONSENSUS SEQUENCE, ESCHERICHIA-COLI, glycoprotein, glycosylation, Helicobacter, INFLUENZAE HMW1 ADHESIN, Life Sciences & Biomedicine, N-linked, Science & Technology, SUBSTRATE-SPECIFICITY, TRANSFERASE |
| الوصف: | N-linked protein glycosylation systems operate in species from all three domains of life. The model bacterial N-linked glycosylation system from Campylobacter jejuni is encoded by pgl genes present at a single chromosomal locus. This gene cluster includes the pglB oligosaccharyltransferase responsible for transfer of glycan from lipid carrier to protein. Although all genomes from species of the Campylobacter genus contain a pgl locus, among the related Helicobacter genus only three evolutionarily related species (H. pullorum, H. canadensis and H. winghamensis) potentially encode N-linked protein glycosylation systems. Helicobacter putative pgl genes are scattered in five chromosomal loci and include two putative oligosaccharyltransferase-encoding pglB genes per genome. We have previously demonstrated the in vitro N-linked glycosylation activity of H. pullorum resulting in transfer of a pentasaccharide to a peptide at asparagine within the sequon (D/E)XNXS/T. In this study, we identified the first H. pullorum N-linked glycoprotein, termed HgpA. Production of histidine-tagged HgpA in the background of insertional knockout mutants of H. pullorum pgl/wbp genes followed by analysis of HgpA glycan structures demonstrated the role of individual gene products in the PglB1-dependent N-linked protein glycosylation pathway. Glycopeptide purification by zwitterionic-hydrophilic interaction liquid chromatography coupled with tandem mass spectrometry identified six glycosites from five H. pullorum proteins, which was consistent with proteins reactive with a polyclonal antiserum generated against glycosylated HgpA. This study demonstrates functioning of a H. pullorum N-linked general protein glycosylation system. |
| نوع الوثيقة: | article in journal/newspaper |
| اللغة: | unknown |
| Relation: | http://hdl.handle.net/10779/DRO/DU:24531076.v3 |
| الاتاحة: | http://hdl.handle.net/10779/DRO/DU:24531076.v3 https://figshare.com/articles/journal_contribution/Functional_analysis_of_the_i_Helicobacter_pullorum_N_i_-linked_protein_glycosylation_system/24531076 |
| Rights: | CC BY 4.0 |
| رقم الانضمام: | edsbas.724EAF96 |
| قاعدة البيانات: | BASE |
| الوصف غير متاح. |