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Guanylate-binding proteins: mechanisms of pattern recognition and antimicrobial functions.
Kirkby, Max; Enosi Tuipulotu, Daniel; Feng, Shouya; Lo Pilato, Jordan; Man, Si Ming.
Afiliación
  • Kirkby M; Division of Immunology and Infectious Disease, The John Curtin School of Medical Research, The Australian National University, Canberra, Australia.
  • Enosi Tuipulotu D; Division of Immunology and Infectious Disease, The John Curtin School of Medical Research, The Australian National University, Canberra, Australia.
  • Feng S; Division of Immunology and Infectious Disease, The John Curtin School of Medical Research, The Australian National University, Canberra, Australia.
  • Lo Pilato J; Division of Immunology and Infectious Disease, The John Curtin School of Medical Research, The Australian National University, Canberra, Australia.
  • Man SM; Division of Immunology and Infectious Disease, The John Curtin School of Medical Research, The Australian National University, Canberra, Australia. Electronic address: siming.man@anu.edu.au.
Trends Biochem Sci ; 48(10): 883-893, 2023 10.
Article en En | MEDLINE | ID: mdl-37567806
Guanylate-binding proteins (GBPs) are a family of intracellular proteins which have diverse biological functions, including pathogen sensing and host defense against infectious disease. These proteins are expressed in response to interferon (IFN) stimulation and can localize and target intracellular microbes (e.g., bacteria and viruses) by protein trafficking and membrane binding. These properties contribute to the ability of GBPs to induce inflammasome activation, inflammation, and cell death, and to directly disrupt pathogen membranes. Recent biochemical studies have revealed that human GBP1, GBP2, and GBP3 can directly bind to the lipopolysaccharide (LPS) of Gram-negative bacteria. In this review we discuss emerging data highlighting the functional versatility of GBPs, with a focus on their molecular mechanisms of pattern recognition and antimicrobial activity.
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Texto completo: 1 Colección: 01-internacional Banco de datos: MEDLINE Asunto principal: Proteínas Portadoras / Antiinfecciosos Límite: Humans Idioma: En Revista: Trends Biochem Sci Año: 2023 Tipo del documento: Article País de afiliación: Australia

Texto completo: 1 Colección: 01-internacional Banco de datos: MEDLINE Asunto principal: Proteínas Portadoras / Antiinfecciosos Límite: Humans Idioma: En Revista: Trends Biochem Sci Año: 2023 Tipo del documento: Article País de afiliación: Australia