Three distinct glycosylation pathways are involved in the decoration of Lactococcus lactis cell wall glycopolymers

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dc.contributor.author Theodorou, Ilias
dc.contributor.author Courtin, Pascal
dc.contributor.author Sadovskaya, Irina
dc.contributor.author Palussière, Simon
dc.contributor.author Fenaille, François
dc.contributor.author Mahony, Jennifer
dc.contributor.author Chapot-Chartier, Marie-Pierre
dc.contributor.author van Sinderen, Douwe
dc.date.accessioned 2020-03-18T10:44:25Z
dc.date.available 2020-03-18T10:44:25Z
dc.date.issued 2020-03-13
dc.identifier.citation Theodorou, I., Courtin, P., Sadovskaya, I., Palussière, S., Fenaille, F., Mahony, J., Chapot-Chartier, M.P. and van Sinderen, D. (2020) ‘Three distinct glycosylation pathways are involved in the decoration of Lactococcus lactis cell wall glycopolymers’, Journal of Biological Chemistry. doi: 10.1074/jbc.RA119.010844 en
dc.identifier.issn 0021-9258
dc.identifier.uri http://hdl.handle.net/10468/9769
dc.identifier.doi 10.1074/jbc.RA119.010844 en
dc.description.abstract Extra-cytoplasmic sugar decoration of glycopolymer components of the bacterial cell wall contributes to their structural diversity. Typically, the molecular mechanism that underpins such a decoration process involves a three-component glycosylation system (TGS) represented by an undecaprenyl-phosphate (Und-P) sugar-activating glycosyltransferase (Und-P GT), a flippase, and a polytopic glycosyltransferase (PolM GT) dedicated to attaching sugar residues to a specific glycopolymer. Here, using bioinformatic analyses, CRISPR-assisted recombineering, structural analysis of cell wall-associated polysaccharides (CWPS) through Maldi-Tof MS and methylation analysis, we report on three such systems in the bacterium Lactococcus lactis. On the basis of sequence similarities, we first identified three gene pairs, csdAB, csdCD, and csdEF, each encoding an Und-P GT and a PolM GT, as potential TGS component candidates. Our experimental results show that csdAB and csdCD are involved in Glc side chain addition on the CWPS components rhamnan and polysaccharide pellicle (PSP), respectively, whereas csdEF plays a role in galactosylation of lipoteichoic acid (LTA). We also identified a potential flippase encoded in the L. lactis genome (llnz_02975, cflA) and confirmed that it participates in the glycosylation of the three cell wall glycopolymers rhamnan, PSP, and LTA, thus indicating that its function is shared by the three TGSs. Finally, we observed that glucosylation of both rhamnan and PSP can increase resistance to bacteriophage predation and that LTA galactosylation alters L. lactis resistance to bacteriocin. en
dc.format.mimetype application/pdf en
dc.language.iso en en
dc.publisher American Society for Biochemistry and Molecular Biology en
dc.rights © 2020, the Authors. Published under license by The American Society for Biochemistry and Molecular Biology, Inc. This is an Open Access article under the CC BY license. This research was originally published in the Journal of Biological Chemistry: Theodorou, I., Courtin, P., Sadovskaya, I., Palussière, S., Fenaille, F., Mahony, J., Chapot-Chartier, M.P. and van Sinderen, D. (2020) ‘Three distinct glycosylation pathways are involved in the decoration of Lactococcus lactis cell wall glycopolymers’, Journal of Biological Chemistry. doi: 10.1074/jbc.RA119.010844 en
dc.rights.uri https://creativecommons.org/licenses/by/4.0/
dc.subject Lactic acid bacteria en
dc.subject Glycopolymer en
dc.subject Phage receptor en
dc.subject Lipoteichoic acid en
dc.subject LTA en
dc.subject Flippase en
dc.subject Peptidoglycan en
dc.subject Glycosylation en
dc.subject Genomics en
dc.subject Glycobiology en
dc.subject Bacteriophage en
dc.subject Cell wall en
dc.subject Glycosyltransferase en
dc.title Three distinct glycosylation pathways are involved in the decoration of Lactococcus lactis cell wall glycopolymers en
dc.type Article (peer-reviewed) en
dc.type Article (preprint) en
dc.internal.authorcontactother Douwe van Sinderen, School of Microbiology and APC Microbiome Ireland, University College Cork, Cork, Ireland. +353-21-490-3000 Email: d.vansinderen@ucc.ie en
dc.internal.availability Full text available en
dc.description.version Published Version en
dc.contributor.funder Science Foundation Ireland en
dc.description.status Peer reviewed en
dc.identifier.journaltitle Journal of Biological Chemistry en
dc.internal.IRISemailaddress d.vansinderen@ucc.ie en
dc.internal.bibliocheck In press. Check volume / issue / page range. Amend citation accordingly. en
dc.relation.project info:eu-repo/grantAgreement/SFI/SFI Investigator Programme/13/IA/1953/IE/Functional analysis of the host adsorption and DNA injection processes of a lactococcal bacteriophage/ en
dc.relation.project info:eu-repo/grantAgreement/SFI/SFI Starting Investigator Research Grant (SIRG)/15/SIRG/3430/IE/Phage-host interactome of the dairy bacterium Streptococcus thermophilus (PHIST)/ en
dc.identifier.eissn 1083-351X


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© 2020, the Authors. Published under license by The American Society for Biochemistry and Molecular Biology, Inc. This is an Open Access article under the CC BY license. This research was originally published in the Journal of Biological Chemistry: Theodorou, I., Courtin, P., Sadovskaya, I., Palussière, S., Fenaille, F., Mahony, J., Chapot-Chartier, M.P. and van Sinderen, D. (2020) ‘Three distinct glycosylation pathways are involved in the decoration of Lactococcus lactis cell wall glycopolymers’, Journal of Biological Chemistry. doi: 10.1074/jbc.RA119.010844 Except where otherwise noted, this item's license is described as © 2020, the Authors. Published under license by The American Society for Biochemistry and Molecular Biology, Inc. This is an Open Access article under the CC BY license. This research was originally published in the Journal of Biological Chemistry: Theodorou, I., Courtin, P., Sadovskaya, I., Palussière, S., Fenaille, F., Mahony, J., Chapot-Chartier, M.P. and van Sinderen, D. (2020) ‘Three distinct glycosylation pathways are involved in the decoration of Lactococcus lactis cell wall glycopolymers’, Journal of Biological Chemistry. doi: 10.1074/jbc.RA119.010844
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