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Sugar coating: bacterial protein glycosylation and host-microbe interactions.
Tan, Felicia Y Y; Tang, Christoph M; Exley, Rachel M.
Afiliação
  • Tan FY; Sir William Dunn School of Pathology, University of Oxford, South Parks Road, Oxford OX1 3RE, UK.
  • Tang CM; Sir William Dunn School of Pathology, University of Oxford, South Parks Road, Oxford OX1 3RE, UK.
  • Exley RM; Sir William Dunn School of Pathology, University of Oxford, South Parks Road, Oxford OX1 3RE, UK. Electronic address: rachel.exley@path.ox.ac.uk.
Trends Biochem Sci ; 40(7): 342-50, 2015 Jul.
Article em En | MEDLINE | ID: mdl-25936979
ABSTRACT
Bacterial surfaces are rich in glycoconjugates such as capsules, lipopolysaccharides, and peptidoglycans. The discovery of prokaryotic protein glycosylation systems has revealed that many bacteria also have the capacity to synthesise a diverse array of protein glycans, in some cases using novel strategies that differ from those of eukaryotes. Despite advances in our understanding of glycan biosynthesis and the proteins that are targets of glycosylation in bacteria, the roles of these modifications are relatively less well explored. We present an overview of bacterial protein glycosylation systems in bacteria that are relevant to human health, and discuss current evidence which indicates that glycosylation of proteins may impact upon fundamental processes such as bacterial motility, adhesion, and the modulation of immune responses.
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Bactérias / Proteínas de Bactérias / Processamento de Proteína Pós-Traducional Limite: Animals / Humans Idioma: En Revista: Trends Biochem Sci Ano de publicação: 2015 Tipo de documento: Article País de afiliação: Reino Unido

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Bactérias / Proteínas de Bactérias / Processamento de Proteína Pós-Traducional Limite: Animals / Humans Idioma: En Revista: Trends Biochem Sci Ano de publicação: 2015 Tipo de documento: Article País de afiliação: Reino Unido