Dataset Information

BEMAP analysis of glycosylated TW10722 YghJ

ABSTRACT: In the present study we have further investigated the extent of YghJ glycosylation and coupled this inherent O-linked protein glycosylation to an increased antigenic potential of YghJ. We have expressed and purified glycosylated YghJ from the ETEC strain TW10722 and performed an in depth BEMAP analysis to identify glycosylated Ser/Thr residues

INSTRUMENT(S): Orbitrap Fusion Lumos

ORGANISM(S): Escherichia Coli

SUBMITTER: Anders Boysen

LAB HEAD: Anders Boysen

PROVIDER: PXD030322 | Pride | 2022-02-17

REPOSITORIES: Pride

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Dataset's files

Source:

			Action	DRS
	LUM2_04768.pdResult	Other
	LUM2_04768.raw	Raw

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Publications

Characterization of Glycosylation-Specific Systemic and Mucosal IgA Antibody Responses to Escherichia coli Mucinase YghJ (SslE).

Riaz Saman S Steinsland Hans H Thorsing Mette M Andersen Ann Z AZ Boysen Anders A Hanevik Kurt K

Frontiers in immunology 20211217

Efforts to develop broadly protective vaccines against pathogenic Escherichia coli are ongoing. A potential antigen candidate for vaccine development is the metalloprotease YghJ, or SslE. YghJ is a conserved mucinase that is immunogenic, heavily glycosylated, and produced by most pathogenic E. coli. To develop efficacious YghJ-based vaccines, there is a need to investigate to what extent potentially protective antibody responses target glycosylated epitopes in YghJ and to describe ...[more]

PMID: 34975849

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Dataset Information

BEMAP analysis of glycosylated TW10722 YghJ

Dataset's files

Publications

Characterization of Glycosylation-Specific Systemic and Mucosal IgA Antibody Responses to <i>Escherichia coli</i> Mucinase YghJ (SslE).

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