A Novel Xylosylphosphotransferase Activity Discovered in Cryptococcus neoformans

Reilly, Morgann C.; Levery, Steven B.; Castle, Sherry A.; Klutts, J. Stacey; Doering, Tamara L.

doi:10.1074/jbc.m109.056226

Cited by 19 publications

(22 citation statements)

References 42 publications

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“…Besides the xylose addition that is mediated by the Cxt proteins, we have discovered a completely distinct and novel activity of C. neoformans that adds xylose-phosphate (Xyl-P) to Man-containing substrates (21). The resulting Xyl-P-Man linkage has not been previously observed in the glycan structures of C. neoformans or any other organism nor has an enzyme with xylosylphosphotransferase activity been described.…”

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confidence: 81%

“…The resulting Xyl-P-Man linkage has not been previously observed in the glycan structures of C. neoformans or any other organism nor has an enzyme with xylosylphosphotransferase activity been described. We have identified and characterized the C. neoformans protein responsible for this activity, xylosylphosphotransferase 1 (Xpt1p (21)). This protein is specific for UDP-Xyl as the reaction donor but readily modifies a variety of Man-containing substrates.…”

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confidence: 99%

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A Xylosylphosphotransferase of Cryptococcus neoformans Acts in Protein O-Glycan Synthesis

Reilly

Aoki

Wang

et al. 2011

Journal of Biological Chemistry

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Cryptococcal meningoencephalitis is an AIDS-defining illness caused by the opportunistic pathogen Cryptococcus neoformans. This organism possesses an elaborate polysaccharide capsule that is unique among pathogenic fungi, and the glycobiology of C. neoformans has been a focus of research in the field. The capsule and other cellular glycans and glycoconjugates have been described, but the machinery responsible for their synthesis remains largely unexplored. We recently discovered Xpt1p, an enzyme with the unexpected activity of generating a xylosephosphate-mannose linkage. We now demonstrate that this novel activity is conserved throughout the C. neoformans species complex, localized to the Golgi apparatus, and functions in the O-glycosylation of proteins. We also present the first survey of O-glycans from C. neoformans.

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confidence: 81%

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confidence: 99%

A Xylosylphosphotransferase of Cryptococcus neoformans Acts in Protein O-Glycan Synthesis

Reilly

Aoki

Wang

et al. 2011

Journal of Biological Chemistry

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“…The 3-O-α-D-mannopyranosyl-α-D-mannopyranosexylosylphosphotransferase is a specific enzyme for UDP-xylose and for the mannose acceptor to form a xylose-1-phosphate-6-mannose linkage. This enzyme was also identified in Heterobasidiomycetes Cryptococcus neoformans [22]. Mannitol-1-phosphate 5-dehydrogenase is a key enzyme in the mannitol cycle, which is commonly found in white-rot basidiomycetes such as Phanerochaete crysosporium and Pleurotus ostreatus [23,24].…”

Section: Resultsmentioning

confidence: 99%

Initial Proteomic Identification of Secreted Proteins of White-Rot Fungus Porodaedalea pini Grown on Liquid Medium

Sunardi¹,

Nakamura²,

Ishiguri³

et al. 2018

Asian J. Chem.

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Porodaedalea pini is a white-rot fungus that attacks conifers and secretes different kinds of extracellular enzymes. To our best of knowledge, this is the first report identifying the secreted proteome of P. pini grown on liquid medium. Some proteins involved in carbohydrate metabolism were identified by peptide mass fingerprinting (PMF) using matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI/TOF/MS). The identified proteins were classified according to their biochemical roles as carbohydrate transport and metabolism, amino acid transport and metabolism, aromatic compound metabolism and oxidative stress responses, cellular processes and signaling and hypothetical proteins. Furthermore, one spot of the proteins in the carbohydrate transport and metabolism categories may be correlated to the hydrolytic enzymes secretion. This protein was homologous to the glycoside hydrolase family 1 and seems to be a β-glucosidase.

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“…The ALL1::HA-tagged strain (where HA is hemagglutinin) was generated using the following strategy (19,20). The ALL1 gene was amplified under its own promoter from RC2 genomic DNA using primers ALL1-prom-F-XbaI and ALL1-HARev (see Table S2 in the supplemental material).…”

Section: Methodsmentioning

confidence: 99%

ALL2 , a Homologue of ALL1 , Has a Distinct Role in Regulating pH Homeostasis in the Pathogen Cryptococcus neoformans

et al. 2016

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Cryptococcus neoformans is a facultative intracellular fungal pathogen that has a polysaccharide capsule and causes life-threatening meningoencephalitis. Its capsule, as well as its ability to survive in the acidic environment of the phagolysosome, contributes to the pathogen's resilience in the host environment. Previously, we reported that downregulation of allergen 1 (ALL1) results in the secretion of a shorter, more viscous exopolysaccharide with less branching and structural complexity, as well as altered iron homeostasis. Now, we report on a homologous coregulated gene, allergen 2 (ALL2). ALL2's function was characterized by generating null mutants in C. neoformans. In contrast to ALL1, loss of ALL2 attenuated virulence in the pulmonary infection model. The all2⌬ mutant shed a less viscous exopolysaccharide and exhibited higher sensitivity to hydrogen peroxide than the wild type, and as a result, the all2⌬ mutant was more resistant to macrophage-mediated killing. Transcriptome analysis further supported the distinct function of these two genes. Unlike ALL1's involvement in iron homeostasis, we now present data on ALL2's unique function in maintaining intracellular pH in low-pH conditions. Thus, our data highlight that C. neoformans, a human-pathogenic basidiomycete, has evolved a unique set of virulence-associated genes that contributes to its resilience in the human niche.

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A Novel Xylosylphosphotransferase Activity Discovered in Cryptococcus neoformans

Cited by 19 publications

References 42 publications

A Xylosylphosphotransferase of Cryptococcus neoformans Acts in Protein O-Glycan Synthesis

A Xylosylphosphotransferase of Cryptococcus neoformans Acts in Protein O-Glycan Synthesis

Initial Proteomic Identification of Secreted Proteins of White-Rot Fungus Porodaedalea pini Grown on Liquid Medium

ALL2 , a Homologue of ALL1 , Has a Distinct Role in Regulating pH Homeostasis in the Pathogen Cryptococcus neoformans

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