Dataset Information

Post-translational modifications of vaccine candidates of Cryptosporidium parvum

ABSTRACT: Here we describe the post translational modifications on vaccine candidate proteins from Cryptosporidium parvum. We have identified O-glycosylated peptides from GP15, GP40, GP900, and a novel mucin-like protein referred to as GP20. In addition, we have discovered that the immune dominant antigen, CP23, contains both N-myristoyl and C-palmitoyl modifications on the N-terminal region of the protein.

INSTRUMENT(S): Q Exactive Plus, LTQ Orbitrap XL ETD

ORGANISM(S): Cryptosporidium Parvum

TISSUE(S): Sporulated Oocyst

SUBMITTER: John Haserick

LAB HEAD: Catherine E. Costello

PROVIDER: PXD005989 | Pride | 2017-08-14

REPOSITORIES: Pride

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Dataset's files

Source:

			Action	DRS
	02-17-2015_WTD_120min_QE+.pride.mgf.gz	Mgf
	02-17-2015_WTD_120min_QE.mgf	Mgf
	02-17-2015_WTD_120min_QE.raw	Raw
	02-17-2015_WTD_120min_QE_raw-10389.svg	Svg
	02-17-2015_WTD_120min_QE_raw-3178.svg	Svg

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Publications

Cryptosporidium parvum vaccine candidates are incompletely modified with O-linked-N-acetylgalactosamine or contain N-terminal N-myristate and S-palmitate.

Haserick John R JR Klein Joshua A JA Costello Catherine E CE Samuelson John J

PloS one 20170808 8

Cryptosporidium parvum (studied here) and Cryptosporidium hominis are important causes of diarrhea in infants and immunosuppressed persons. C. parvum vaccine candidates, which are on the surface of sporozoites, include glycoproteins with Ser- and Thr-rich domains (Gp15, Gp40, and Gp900) and a low complexity, acidic protein (Cp23). Here we used mass spectrometry to determine that O-linked GalNAc is present in dense arrays on a glycopeptide with consecutive Ser derived from Gp40 and on glycopeptid ...[more]

PMID: 28792526

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