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1.
Bio Protoc ; 8(8): e2802, 2018 Apr 20.
Artigo em Inglês | MEDLINE | ID: mdl-34286021

RESUMO

Enteroaggregative Escherichia coli (EAEC) is a recognized cause of acute diarrhea among both children and adults worldwide. EAEC strains are characterized by the presence of aggregative adherence fimbriae (AAF), which play a key role in pathogenesis by mediating attachment to the intestinal mucosa and by triggering host inflammatory responses. The aggregative adherence fimbria II (AAF/II) is the most important adherence factor of EAEC prototype strain 042 (EAEC042) to intestinal cells. Multiple receptors for AAF/II on epithelial cells have been identified including the transmembrane signaling mucin Muc1. This protocol describes a method to measure adherence of EAEC strains to HEK293 cells expressing the Muc1 glycoprotein.

2.
PLoS One ; 9(9): e107920, 2014.
Artigo em Inglês | MEDLINE | ID: mdl-25251283

RESUMO

The serine protease autotransporter from Enterobacteriaceae (SPATE) family, which number more than 25 proteases with apparent diverse functions, have been phylogenetically divided into two distinct classes, designated 1 and 2. We recently demonstrated that Pic and Tsh, two members of the class-2 SPATE family produced by intestinal and extraintestinal pathogenic E. coli, were able to cleave a number of O-glycosylated proteins on neutrophils and lymphocytes resulting in impaired leukocyte functions. Here we show that most members of the class-2 SPATE family have lectin-like properties and exhibit differential protease activity reliant on glycoprotein type and cell lineage. Protease activity was seen in virtually all tested O-glycosylated proteins including CD34, CD55, CD164, TIM1, TIM3, TIM4 and C1-INH. We also show that although SPATE proteins bound and cleaved glycoproteins more efficiently on granulocytes and monocytes, they also targeted glycoproteins on B, T and natural killer lymphocytes. Finally, we found that the characteristic domain-2 of class-2 SPATEs is not required for glycoprotease activity, but single amino acid mutations in Pic domain-1 to those residues naturally occurring in domain-1 of SepA, were sufficient to hamper Pic glycoprotease activity. This study shows that most class-2 SPATEs have redundant activities and suggest that they may function as immunomodulators at several levels of the immune system.


Assuntos
Infecções por Enterobacteriaceae/imunologia , Enterobacteriaceae/enzimologia , Enterobacteriaceae/fisiologia , Interações Hospedeiro-Patógeno , Leucócitos/microbiologia , Serina Proteases/imunologia , Sequência de Aminoácidos , Linhagem Celular , Células Cultivadas , Enterobacteriaceae/genética , Enterobacteriaceae/imunologia , Infecções por Enterobacteriaceae/metabolismo , Glicoproteínas/análise , Glicoproteínas/imunologia , Glicoproteínas/metabolismo , Humanos , Leucócitos/imunologia , Leucócitos/metabolismo , Modelos Moleculares , Dados de Sequência Molecular , Filogenia , Proteólise , Alinhamento de Sequência , Serina Proteases/análise , Serina Proteases/genética , Serina Proteases/metabolismo
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