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- W3206658078 endingPage "875" @default.
- W3206658078 startingPage "875" @default.
- W3206658078 abstract "Protein glycosylation is a highly conserved post-translational modification among organisms. It plays fundamental roles in many biological processes, ranging from protein trafficking and cell adhesion to host-pathogen interactions. According to the amino acid side chain atoms to which glycans are linked, protein glycosylation can be divided into two major categories: N-glycosylation and O-glycosylation. However, there are other types of modifications such as the addition of GPI to the C-terminal end of the protein. Besides the importance of glycoproteins in biological functions, they are a major component of the fungal cell wall and plasma membrane and contribute to pathogenicity, virulence, and recognition by the host immunity. Given that this structure is absent in host mammalian cells, it stands as an attractive target for developing selective compounds for the treatment of fungal infections. This review focuses on describing the relationship between protein glycosylation and the host-immune interaction in medically relevant fungal species." @default.
- W3206658078 created "2021-10-25" @default.
- W3206658078 creator A5042379792 @default.
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- W3206658078 creator A5066366882 @default.
- W3206658078 creator A5089035015 @default.
- W3206658078 creator A5089100795 @default.
- W3206658078 date "2021-10-18" @default.
- W3206658078 modified "2023-10-15" @default.
- W3206658078 title "Role of Protein Glycosylation in Interactions of Medically Relevant Fungi with the Host" @default.
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