Role of Protein Glycosylation in Interactions of Medically Relevant Fungi with the Host

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 li...
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Autor*in:	Manuela Gómez-Gaviria [verfasserIn] Ana P. Vargas-Macías [verfasserIn] Laura C. García-Carnero [verfasserIn] Iván Martínez-Duncker [verfasserIn] Héctor M. Mora-Montes [verfasserIn]

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2021

Schlagwörter:	glycosylphosphatidylinositol anchors host–fungus interaction glycoproteins virulence

Übergeordnetes Werk:	In: Journal of Fungi - MDPI AG, 2015, 7(2021), 10, p 875
Übergeordnetes Werk:	volume:7 ; year:2021 ; number:10, p 875

Links:	Link aufrufen Link aufrufen Link aufrufen Journal toc

DOI / URN:	10.3390/jof7100875

Katalog-ID:	DOAJ009002170

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520			\|a 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: <i<N-</i<glycosylation and <i<O-</i<glycosylation. However, there are other types of modifications such as the addition of GPI to the <i<C-</i<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.
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allfieldsSound	10.3390/jof7100875 doi (DE-627)DOAJ009002170 (DE-599)DOAJ8096be1664a84f8b84b7ff212a6e33b5 DE-627 ger DE-627 rakwb eng QH301-705.5 Manuela Gómez-Gaviria verfasserin aut Role of Protein Glycosylation in Interactions of Medically Relevant Fungi with the Host 2021 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier 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: <i<N-</i<glycosylation and <i<O-</i<glycosylation. However, there are other types of modifications such as the addition of GPI to the <i<C-</i<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. <i<N</i<-glycosylation <i<O</i<-glycosylation glycosylphosphatidylinositol anchors host–fungus interaction glycoproteins virulence Biology (General) Ana P. Vargas-Macías verfasserin aut Laura C. García-Carnero verfasserin aut Iván Martínez-Duncker verfasserin aut Héctor M. Mora-Montes verfasserin aut In Journal of Fungi MDPI AG, 2015 7(2021), 10, p 875 (DE-627)796588538 (DE-600)2784229-0 2309608X nnns volume:7 year:2021 number:10, p 875 https://doi.org/10.3390/jof7100875 kostenfrei https://doaj.org/article/8096be1664a84f8b84b7ff212a6e33b5 kostenfrei https://www.mdpi.com/2309-608X/7/10/875 kostenfrei https://doaj.org/toc/2309-608X Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 7 2021 10, p 875
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callnumber-first	Q - Science
author	Manuela Gómez-Gaviria
spellingShingle	Manuela Gómez-Gaviria misc QH301-705.5 misc <i<N</i<-glycosylation misc <i<O</i<-glycosylation misc glycosylphosphatidylinositol anchors misc host–fungus interaction misc glycoproteins misc virulence misc Biology (General) Role of Protein Glycosylation in Interactions of Medically Relevant Fungi with the Host
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topic_title	QH301-705.5 Role of Protein Glycosylation in Interactions of Medically Relevant Fungi with the Host <i<N</i<-glycosylation <i<O</i<-glycosylation glycosylphosphatidylinositol anchors host–fungus interaction glycoproteins virulence
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title	Role of Protein Glycosylation in Interactions of Medically Relevant Fungi with the Host
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title_full	Role of Protein Glycosylation in Interactions of Medically Relevant Fungi with the Host
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title_sort	role of protein glycosylation in interactions of medically relevant fungi with the host
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title_auth	Role of Protein Glycosylation in Interactions of Medically Relevant Fungi with the Host
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: <i<N-</i<glycosylation and <i<O-</i<glycosylation. However, there are other types of modifications such as the addition of GPI to the <i<C-</i<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.
abstractGer	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: <i<N-</i<glycosylation and <i<O-</i<glycosylation. However, there are other types of modifications such as the addition of GPI to the <i<C-</i<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.
abstract_unstemmed	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: <i<N-</i<glycosylation and <i<O-</i<glycosylation. However, there are other types of modifications such as the addition of GPI to the <i<C-</i<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.
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title_short	Role of Protein Glycosylation in Interactions of Medically Relevant Fungi with the Host
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Role of Protein Glycosylation in Interactions of Medically Relevant Fungi with the Host

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