The Salmonella enterica giant adhesin SiiE binds to polarized epithelial cells in a lectin-like manner.
作者： Carolin Wagner , Britta Barlag , Roman G. Gerlach , Jörg Deiwick , Michael Hensel
DOI: 10.1111/CMI.12253
关键词:
摘要: Summary The invasion of polarized epithelial cells by Salmonella enterica requires the cooperative activity pathogenicity island (SPI) 1-encoded type III secretion system (T3SS) and SPI4-encoded giant non-fimbrial adhesin SiiE. SiiE is a highly repetitive protein composed 53 bacterial Ig (BIg) domains mediates binding to apical side cells. We analysed properties observed lectin-like activity. SiiE-dependent cell can be ablated chemical or enzymatic deglycosylation. Lectin blockade experiments revealed that specific for glycostructures with terminal N-acetyl-glucosamine (GlcNAc) and/or α 2,3-linked sialic acid. In line these data, we found SiiE-expressing bind GlcNAc polymer chitin. Various recombinant fragments were host binding. C-terminal portions intensity increases number BIg present in proteins. Based on results, propose multiple interactions per molecule glycoproteins glycosylated phospholipids membrane Thisintimate enables subsequent function SPI1-T3SS, resulting invasion.
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