Artículo
Type III Secretion Effectors with Arginine N-Glycosyltransferase Activity
Autor/es | Araujo Garrido, Juan Luis
Bernal Bayard, Joaquín Ramos Morales, Francisco |
Departamento | Universidad de Sevilla. Departamento de Genética |
Fecha de publicación | 2020 |
Fecha de depósito | 2020-03-09 |
Publicado en |
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Resumen | Type III secretion systems are used by many Gram-negative bacterial pathogens to inject proteins, known as effectors, into the cytosol of host cells. These virulence factors interfere with a diverse array of host signal ... Type III secretion systems are used by many Gram-negative bacterial pathogens to inject proteins, known as effectors, into the cytosol of host cells. These virulence factors interfere with a diverse array of host signal transduction pathways and cellular processes. Many effectors have catalytic activities to promote post-translational modifications of host proteins. This review focuses on a family of effectors with glycosyltransferase activity that catalyze addition of N-acetyl-d-glucosamine to specific arginine residues in target proteins, leading to reduced NF-κB pathway activation and impaired host cell death. This family includes NleB from Citrobacter rodentium, NleB1 and NleB2 from enteropathogenic and enterohemorrhagic Escherichia coli, and SseK1, SseK2, and SseK3 from Salmonella enterica. First, we place these effectors in the general framework of the glycosyltransferase superfamily and in the particular context of the role of glycosylation in bacterial pathogenesis. Then, we provide detailed information about currently known members of this family, their role in virulence, and their targets |
Agencias financiadoras | Ministerio de Economia, Industria y Competitividad (MINECO). España Agencia Estatal de Investigación. España European Regional Development Fund European Union (UE). H2020 |
Identificador del proyecto | SAF2016‐75365‐R
No 842629 |
Cita | Araujo Garrido, J.L., Bernal Bayard, J. y Ramos Morales, F. (2020). Type III Secretion Effectors with Arginine N-Glycosyltransferase Activity. Microorganisms, 8 (3), 1-23. |
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pubmicroorganisms-08-00357.pdf | 1.965Mb | [PDF] | Ver/ | |