PXD033468

PXD033468 is an original dataset announced via ProteomeXchange.

Title	Discovery and characterization of a new class of O-linking oligosaccharyltransferase from bacteria in the Moraxellaceae family
Description	Bacterial protein glycosylation can be mediated by oligosaccharyltransferases (OTases) that transfer a preassembled lipid-linked oligosaccharide or polysaccharide en bloc to acceptor proteins. O-linking OTases transfer O-antigen or capsular polysaccharides to the side chains of serine or threonine residues. Three major families of bacterial O-linking OTases have been described so far: PglL, PglS, and TfpO. TfpO enzymes are limited to transferring only short glycans whereas there are no clear upper limits for the other two families. Herein, we describe the discovery of a novel family of bacterial O-linking OTases from Moraxellacea bacteria that are similar in size and sequence to TfpO enzymes but can transfer long-chain bacterial glycans to acceptor proteins. Bioinformatic analyses show that these enzymes cluster in different clades than known bacterial OTases. Using a representative enzyme from Moraxella osloensis termed TfpMMo, we determine that the enzyme glycosylates the C-terminal amino acid side chain of a pilin protein and find that pilin fragments as short as three amino acids are substrates for the OTase. The ability of TfpMMo to transfer long-chain polysaccharide shows that this ability is not limited to the PglS and PglL families. TfpMMo is also shown to have broad substrate specificity and can transfer diverse glycans including those with glucose, galactose, or 2-N-acetyl sugars at the reducing end. The glycan substrate promiscuity of TfpMMo could allow this enzyme to be used to produce bacterial glycoconjugate vaccines. The discovery of a new class of O-linking OTase furthers our understanding of the mechanisms that underly glycan specificity by these and other O-linking OTases and enables more comparative studies of this important enzyme family.
HostingRepository	PRIDE
AnnounceDate	2022-10-13
AnnouncementXML	Submission_2022-10-13_02:50:22.883.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	NichollasScott
SpeciesList	scientific name: Moraxella osloensis; NCBI TaxID: 34062;
ModificationList	complex glycosylation
Instrument	Orbitrap Fusion Lumos

Revision	Datetime	Status	ChangeLog Entry
0	2022-04-27 03:46:35	ID requested
⏵ 1	2022-10-13 02:50:23	announced

Dataset with its publication pending

submitter keyword: glycosylation, M. osloensis

Christian M.Harding
contact affiliation	Omniose/VaxNewMo, St. Louis, MO 63110
contact email	christian.harding@vaxnewmo.com
lab head
NichollasScott
contact affiliation	University of Melbourne
contact email	nichollas.scott@unimelb.edu.au
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD033468
     1. Label: PRIDE project
     2. Name: Discovery and characterization of a new class of O-linking oligosaccharyltransferase from bacteria in the Moraxellaceae family