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- W3024054972 abstract "We previously reported that the outer mannose chains of N -glycans are dispensable for the virulence of C. neoformans , which is in stark contrast to findings for the other human-pathogenic yeast, Candida albicans . Here, we present evidence that an intact core N -glycan structure is required for C. neoformans pathogenicity by systematically analyzing alg3Δ, alg9Δ , and alg12Δ strains that have defects in lipid-linked N- glycan assembly and in in vivo virulence. The alg null mutants producing truncated core N -glycans were defective in inducing host cell death after phagocytosis, which is triggered as a mechanism of pulmonary escape and dissemination of C. neoformans , thus becoming inactive in causing fatal infection. The results clearly demonstrated the critical features of the N -glycan structure in mediating the interaction with host cells during fungal infection. The delineation of the roles of protein glycosylation in fungal pathogenesis not only provides insight into the glycan-based fungal infection mechanism but also will aid in the development of novel antifungal agents." @default.
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- W3024054972 date "2020-06-30" @default.
- W3024054972 modified "2023-09-24" @default.
- W3024054972 title "Core <i>N</i> -Glycan Structures Are Critical for the Pathogenicity of Cryptococcus neoformans by Modulating Host Cell Death" @default.
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- W3024054972 doi "https://doi.org/10.1128/mbio.00711-20" @default.
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