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Microbiology
3 Results
- Research ArticleOpen Access
Cryptococcus neoformans melanization incorporates multiple catecholamines to produce polytypic melanin
Journal of Biological ChemistryVol. 298Issue 1101519Published online: December 20, 2021- Rosanna P. Baker
- Christine Chrissian
- Ruth E. Stark
- Arturo Casadevall
Cited in Scopus: 3Melanin is a major virulence factor in pathogenic fungi that enhances the ability of fungal cells to resist immune clearance. Cryptococcus neoformans is an important human pathogenic fungus that synthesizes melanin from exogenous tissue catecholamine precursors during infection, but the type of melanin made in cryptococcal meningoencephalitis is unknown. We analyzed the efficacy of various catecholamines found in brain tissue in supporting melanization using animal brain tissue and synthetic catecholamine mixtures reflecting brain tissue proportions. - Molecular BiophysicsOpen Access
Solid-state NMR spectroscopy identifies three classes of lipids in Cryptococcus neoformans melanized cell walls and whole fungal cells
Journal of Biological ChemistryVol. 295Issue 44p15083–15096Published online: August 28, 2020- Christine Chrissian
- Emma Camacho
- John E. Kelly
- Hsin Wang
- Arturo Casadevall
- Ruth E. Stark
Cited in Scopus: 13A primary virulence-associated trait of the opportunistic fungal pathogen Cryptococcus neoformans is the production of melanin pigments that are deposited into the cell wall and interfere with the host immune response. Previously, our solid-state NMR studies of isolated melanized cell walls (melanin “ghosts”) revealed that the pigments are strongly associated with lipids, but their identities, origins, and potential roles were undetermined. Herein, we exploited spectral editing techniques to identify and quantify the lipid molecules associated with pigments in melanin ghosts. - ImmunologyOpen Access
A Monoclonal Antibody to Cryptococcus neoformans Glucuronoxylomannan Manifests Hydrolytic Activity for Both Peptides and Polysaccharides
Journal of Biological ChemistryVol. 292Issue 2p417–434Published online: November 21, 2016- Anthony Bowen
- Maggie P. Wear
- Radames J.B. Cordero
- Stefan Oscarson
- Arturo Casadevall
Cited in Scopus: 27Studies in the 1980s first showed that some natural antibodies were “catalytic” and able to hydrolyze peptide or phosphodiester bonds in antigens. Many naturally occurring catalytic antibodies have since been isolated from human sera and associated with positive and negative outcomes in autoimmune disease and infection. The function and prevalence of these antibodies, however, remain unclear. A previous study suggested that the 18B7 monoclonal antibody against glucuronoxylomannan (GXM), the major component of the Cryptococcus neoformans polysaccharide capsule, hydrolyzed a peptide antigen mimetic.