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Surface Protein Hexosylation in Natural and Synthetic Minimal Genome Bacteria

ABSTRACT: This study describes surface protein hexosylation in Mycoplasma genitalium, a human urogenital pathogen with a 580-kbp genome; the ruminant pathogen Mycoplasma mycoides subsp. capri; and JCVI-syn3A, a bacterium with a synthetic minimal M. mycoides 543-kbp gene set for growth under axenic conditions. Previous work from our group described a surface protein glycosylation system in the murine pathogens M. pulmonis and M. arthritidis that utilizes hexoses cleaved from oligo-/polysaccharides as glycosyl donors and does not utilize a consensus sequence for glycosyl acceptors. As we have been unable to find a glycosylation knockout while screening mycoplasmas, we hypothesized the hexosylation system was active in these minimal genome mycoplasmas as well as JCVI-Syn3A's M. mycodies parent organism. Our data indicates hexosylation is maintaned in these organisms, and remarkably, the available pool of glycosyl acceptors includes aspartic acid and glutamic acid.

INSTRUMENT(S):

ORGANISM(S): Mycoplasmoides Genitalium G37 Synthetic Bacterium Jcvi-syn3a Mycoplasma Mycoides Subsp. Capri Str. Gm12

SUBMITTER: John Sanford

LAB HEAD: Thomas Prescott

PROVIDER: PXD057584 | Pride | 2025-08-01

REPOSITORIES: Pride

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			Action	DRS
	MgenHexSTYNQ.db.mzidentml_1_1_0.xml	Mzid
	MgenHexSTYNQ.spider.mzidentml_1_1_0.xml	Mzid
	MgenHexSTYNQDE.db.mzidentml_1_1_0.xml	Mzid
	MgenHexSTYNQDE.spider.mzidentml_1_1_0.xml	Mzid
	MgenPTM.db.mzidentml_1_1_0.xml	Mzid

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