دورية أكاديمية
أعرض في EDS

Sculpting the Bacterial O -Glycoproteome: Functional Analyses of Orthologous Oligosaccharyltransferases with Diverse Targeting Specificities.

التفاصيل البيبلوغرافية
العنوان: Sculpting the Bacterial O -Glycoproteome: Functional Analyses of Orthologous Oligosaccharyltransferases with Diverse Targeting Specificities.
المؤلفون: Hadjineophytou C; Department of Biosciences, Section for Genetics and Evolutionary Biology, University of Oslogrid.5510.1, Oslo, Norway., Anonsen JH; Department of Biosciences, Section for Genetics and Evolutionary Biology, University of Oslogrid.5510.1, Oslo, Norway., Svingerud T; Department of Biosciences, Section for Genetics and Evolutionary Biology, University of Oslogrid.5510.1, Oslo, Norway., Mortimer TD; Department of Immunology and Infectious Diseases, Harvard T. H. Chan School of Public Health, Boston, Massachusetts, USA., Grad YH; Department of Immunology and Infectious Diseases, Harvard T. H. Chan School of Public Health, Boston, Massachusetts, USA.; Division of Infectious Diseases, Brigham and Women's Hospital and Harvard Medical School, Boston, Massachusetts, USA., Scott NE; Department of Microbiology and Immunology, University of Melbourne at the Peter Doherty Institute for Infection and Immunity, Melbourne, Australia., Koomey M; Department of Biosciences, Section for Genetics and Evolutionary Biology, University of Oslogrid.5510.1, Oslo, Norway.; Department of Biosciences, Centre for Ecological and Evolutionary Synthesis, University of Oslogrid.5510.1, Oslo, Norway.
المصدر: MBio [mBio] 2022 Jun 28; Vol. 13 (3), pp. e0379721. Date of Electronic Publication: 2022 Apr 26.
نوع المنشور: Journal Article; Research Support, Non-U.S. Gov't
اللغة: English
بيانات الدورية: Publisher: American Society for Microbiology Country of Publication: United States NLM ID: 101519231 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 2150-7511 (Electronic) NLM ISO Abbreviation: mBio Subsets: MEDLINE
أسماء مطبوعة: Original Publication: Washington, D.C. : American Society for Microbiology
مواضيع طبية MeSH: Bacterial Proteins*/metabolism , Hexosyltransferases*/metabolism , Membrane Proteins*/metabolism , Neisseria meningitidis*/genetics , Neisseria meningitidis*/metabolism, Fimbriae Proteins/metabolism ; Fimbriae, Bacterial/genetics ; Fimbriae, Bacterial/metabolism ; Glycoproteins/genetics ; Glycoproteins/metabolism ; Neisseria gonorrhoeae/genetics ; Neisseria gonorrhoeae/metabolism
مستخلص: Protein glycosylation systems are widely recognized in bacteria, including members of the genus Neisseria . In most bacterial species, the molecular mechanisms and evolutionary contexts underpinning target protein selection and the glycan repertoire remain poorly understood. Broad-spectrum O -linked protein glycosylation occurs in all human-associated species groups within the genus Neisseria , but knowledge of their individual glycoprotein repertoires is limited. Interestingly, PilE, the pilin subunit of the type IV pilus (Tfp) colonization factor, is glycosylated in Neisseria gonorrhoeae and Neisseria meningitidis but not in the deeply branching species N. elongata subsp. glycolytica . To examine this in more detail, we assessed PilE glycosylation status across the genus and found that PilEs of commensal clade species are not modified by the gonococcal PglO oligosaccharyltransferase. Experiments using PglO oligosaccharyltransferases from across the genus expressed in N. gonorrhoeae showed that although all were capable of broad-spectrum protein glycosylation, those from a deep-branching group of commensals were unable to support resident PilE glycosylation. Further glycoproteomic analyses of these strains using immunoblotting and mass spectrometry revealed other proteins differentially targeted by otherwise remarkably similar oligosaccharyltransferases. Finally, we generated pglO allelic chimeras that begin to localize PglO protein domains associated with unique substrate targeting activities. These findings reveal previously unappreciated differences within the protein glycosylation systems of highly related bacterial species. We propose that the natural diversity manifest in the neisserial protein substrates and oligosaccharyltransferases has significant potential to inform the structure-function relationships operating in these and related bacterial protein glycosylation systems. IMPORTANCE Although general protein glycosylation systems have been well recognized in prokaryotes, the processes governing their distribution, function, and evolution remain poorly understood. Here, we have begun to address these gaps in knowledge by comparative analyses of broad-spectrum O -linked protein glycosylation manifest in species within the genus Neisseria that strictly colonize humans. Using N. gonorrhoeae as a well-defined model organism in conjunction with comparative genomics, intraspecies gene complementation, and glycoprotein phenotyping, we discovered clear differences in both glycosylation susceptibilities and enzymatic targeting activities of otherwise largely conserved proteins. These findings reveal previously unappreciated differences within the protein glycosylation systems of highly related bacterial species. We propose that the natural diversity manifest within Neisseria species has significant potential to elucidate the structure-function relationships operating in these and related systems and to inform novel approaches to applied glycoengineering strategies.
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معلومات مُعتمدة: United Kingdom WT_ Wellcome Trust; R01 AI132606 United States AI NIAID NIH HHS
فهرسة مساهمة: Keywords: Neisseria; evolution; glycoproteins; oligosaccharides; pili
المشرفين على المادة: 0 (Bacterial Proteins)
0 (Glycoproteins)
0 (Membrane Proteins)
147680-16-8 (Fimbriae Proteins)
EC 2.4.1.- (Hexosyltransferases)
EC 2.4.99.18 (dolichyl-diphosphooligosaccharide - protein glycotransferase)
تواريخ الأحداث: Date Created: 20220426 Date Completed: 20220630 Latest Revision: 20231003
رمز التحديث: 20240628
مُعرف محوري في PubMed: PMC9239064
DOI: 10.1128/mbio.03797-21
PMID: 35471082
قاعدة البيانات: MEDLINE
الوصف
تدمد:2150-7511
DOI:10.1128/mbio.03797-21