Effects of altered N-glycan structures of Cryptococcus neoformans mannoproteins, MP98 (Cda2) and MP84 (Cda3), on interaction with host cells
DC Field | Value | Language |
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dc.contributor.author | Lee, Su-Bin | - |
dc.contributor.author | Mota, Catia | - |
dc.contributor.author | Thak, Eun Jung | - |
dc.contributor.author | Kim, Jungho | - |
dc.contributor.author | Son, Ye Ji | - |
dc.contributor.author | Oh, Doo-Byoung | - |
dc.contributor.author | Kang, Hyun Ah | - |
dc.date.accessioned | 2023-03-16T04:41:00Z | - |
dc.date.available | 2023-03-16T04:41:00Z | - |
dc.date.issued | 2023-01 | - |
dc.identifier.issn | 2045-2322 | - |
dc.identifier.uri | https://scholarworks.bwise.kr/cau/handle/2019.sw.cau/66278 | - |
dc.description.abstract | Cryptococcus neoformans is an opportunistic human fungal pathogen causing lethal meningoencephalitis. It has several cell wall mannoproteins (MPs) identified as immunoreactive antigens. To investigate the structure and function of N-glycans assembled on cryptococcal cell wall MPs in host cell interactions, we purified MP98 (Cda2) and MP84 (Cda3) expressed in wild-type (WT) and N-glycosylation-defective alg3 mutant (alg3Δ) strains. HPLC and MALDI-TOF analysis of the MP proteins from the WT revealed protein-specific glycan structures with different extents of hypermannosylation and xylose/xylose phosphate addition. In alg3Δ, MP98 and MP84 had truncated core N-glycans, containing mostly five and seven mannoses (M5 and M7 forms), respectively. In vitro adhesion and uptake assays indicated that the altered core N-glycans did not affect adhesion affinities to host cells although the capacity to induce the immune response of bone-marrow derived dendritic cells (BMDCs) decreased. Intriguingly, the removal of all N-glycosylation sites on MP84 increased adhesion to host cells and enhanced the induction of cytokine secretion from BMDCs compared with that on MP84 carrying WT N-glycans. Therefore, the structure-dependent effects of N-glycans suggested their complex roles in modulating the interaction of MPs with host cells to avoid nonspecific adherence to host cells and host immune response hyperactivation. © 2023, The Author(s). | - |
dc.language | 영어 | - |
dc.language.iso | ENG | - |
dc.publisher | Nature Research | - |
dc.title | Effects of altered N-glycan structures of Cryptococcus neoformans mannoproteins, MP98 (Cda2) and MP84 (Cda3), on interaction with host cells | - |
dc.type | Article | - |
dc.identifier.doi | 10.1038/s41598-023-27422-9 | - |
dc.identifier.bibliographicCitation | Scientific Reports, v.13, no.1 | - |
dc.description.isOpenAccess | Y | - |
dc.identifier.wosid | 000985396000065 | - |
dc.identifier.scopusid | 2-s2.0-85146820230 | - |
dc.citation.number | 1 | - |
dc.citation.title | Scientific Reports | - |
dc.citation.volume | 13 | - |
dc.type.docType | Article | - |
dc.publisher.location | 영국 | - |
dc.subject.keywordPlus | LINKED GLYCOSYLATION | - |
dc.subject.keywordPlus | CHITIN DEACETYLASES | - |
dc.subject.keywordPlus | LECTIN RECEPTORS | - |
dc.subject.keywordPlus | DISSEMINATION | - |
dc.subject.keywordPlus | RECOGNITION | - |
dc.subject.keywordPlus | MECHANISMS | - |
dc.subject.keywordPlus | INDUCTION | - |
dc.subject.keywordPlus | RESPONSES | - |
dc.subject.keywordPlus | PATHWAY | - |
dc.subject.keywordPlus | PROTEIN | - |
dc.relation.journalResearchArea | Science & Technology - Other Topics | - |
dc.relation.journalWebOfScienceCategory | Multidisciplinary Sciences | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
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