The<i>S</i><i>almonella enterica</i>giant adhesin SiiE binds to polarized epithelial cells in a lectin-like manner

Wagner, Carolin; Barlag, Britta; Gerlach, Roman G.; Deiwick, Jörg; Hensel, Michael

doi:10.1111/cmi.12253

Cited by 37 publications

(34 citation statements)

References 40 publications

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“…We found that an adhesive but invasion-deficient strain was randomly distributed on the apical surface. Our previous analysis of the binding specificity of SiiE also did not indicate preferential binding to subpopulations of polarized cells (34). Thus, we exclude heterogeneity in adhesion to polarized cells as a cause of the formation of clusters.…”

Section: Discussionmentioning

confidence: 48%

Salmonella enterica Invasion of Polarized Epithelial Cells Is a Highly Cooperative Effort

et al. 2014

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bThe invasion of polarized epithelial cells by Salmonella enterica requires the cooperative activity of the Salmonella pathogenicity island 1 (SPI1)-encoded type III secretion system (T3SS) and the SPI4-encoded adhesin SiiE. The invasion of polarized cells is more efficient than that of nonpolarized cells, and we observed the formation of clusters of bacteria on infected cells. Here we demonstrate that the invasion of polarized cells is a highly cooperative activity. Using a novel live-cell imaging approach, we visualized the cooperative entry of multiple bacteria into ruffles induced on the apical surfaces of polarized cells. The induction of membrane ruffles by activity of Salmonella enables otherwise noninvasive mutant strains to enter polarized host cells. Bacterial motility and chemotaxis were of lower importance for cooperativity in polarized-cell invasion. We propose that cooperative invasion is a key factor for the very efficient entry into polarized cells and a factor contributing to epithelial damage and intestinal inflammation.

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Section: Discussionmentioning

confidence: 48%

Salmonella enterica Invasion of Polarized Epithelial Cells Is a Highly Cooperative Effort

et al. 2014

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“…Although Ca 2+ ions promote SiiE secretion and folding, we do not assume that they are also directly involved into binding to the target structure. SiiE binds to GlcNAc- and sialic acid-containing structures [5]. Griessl et al .…”

Section: Discussionmentioning

confidence: 99%

“…SiiE, a 595 kDa non-fimbrial adhesin, is the only known substrate for the SPI4-T1SS [4]. SiiE mediates the first intimate contact to the host cell through binding to glycostructures containing N-acetyl-glucosamine and/or α2,3-linked sialic acid [5]. This contact positions the SPI1-T3SS to efficiently translocate effector proteins which lead to actin remodeling and macropinocytosis of the bacteria.…”

Section: Introductionmentioning

confidence: 99%

Structural and functional dissection reveals distinct roles of Ca2+-binding sites in the giant adhesin SiiE of Salmonella enterica

et al. 2017

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The giant non-fimbrial adhesin SiiE of Salmonella enterica mediates the first contact to the apical site of epithelial cells and enables subsequent invasion. SiiE is a 595 kDa protein composed of 53 repetitive bacterial immunoglobulin (BIg) domains and the only known substrate of the SPI4-encoded type 1 secretion system (T1SS). The crystal structure of BIg50-52 of SiiE revealed two distinct Ca2+-binding sites per BIg domain formed by conserved aspartate or glutamate residues. In a mutational analysis Ca2+-binding sites were disrupted by aspartate to serine exchange at various positions in the BIg domains of SiiE. Amounts of secreted SiiE diminish with a decreasing number of intact Ca2+-binding sites. BIg domains of SiiE contain distinct Ca2+-binding sites, with type I sites being similar to other T1SS-secreted proteins and type II sites newly identified in SiiE. We functionally and structurally dissected the roles of type I and type II Ca2+-binding sites in SiiE, as well as the importance of Ca2+-binding sites in various positions of SiiE. Type I Ca2+-binding sites were critical for efficient secretion of SiiE and a decreasing number of type I sites correlated with reduced secretion. Type II sites were less important for secretion, stability and surface expression of SiiE, however integrity of type II sites in the C-terminal portion was required for the function of SiiE in mediating adhesion and invasion.

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“…Protein structure prediction revealed that these internal repeats may have a structure similar to that of the bacterial immunoglobulin-like domain group 3 (BIg 3) repeats found in another nonfimbrial adhesin of S. enterica, SiiE (57). These immunoglobulin folds mediate protein ligand interactions, which endow SiiE with adhesive properties (65). In addition, these immunoglobulin folds, coupled with Ca 2ϩ binding, could also promote SiiE length extension (57), bringing it into proximity with its cognate receptor on the host cell.…”

Section: Discussionmentioning

confidence: 99%

A Conserved PapB Family Member, TosR, Regulates Expression of the Uropathogenic Escherichia coli RTX Nonfimbrial Adhesin TosA while Conserved LuxR Family Members TosE and TosF Suppress Motility

2014

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A heterogeneous subset of extraintestinal pathogenic Escherichia coli (ExPEC) strains, referred to as uropathogenic E. coli (UPEC), causes most uncomplicated urinary tract infections. However, no core set of virulence factors exists among UPEC strains. Instead, the focus of the analysis of urovirulence has shifted to studying broad classes of virulence factors and the interactions between them. For example, the RTX nonfimbrial adhesin TosA mediates adherence to host cells derived from the upper urinary tract. The associated tos operon is well expressed in vivo but poorly expressed in vitro and encodes TosCBD, a predicted type 1 secretion system. TosR and TosEF are PapB and LuxR family transcription factors, respectively; however, no role has been assigned to these potential regulators. Thus, the focus of this study was to determine how TosR and TosEF regulate tosA and affect the reciprocal expression of adhesins and flagella. Among a collection of sequenced UPEC strains, 32% (101/317) were found to encode TosA, and nearly all strains (91% [92/101]) simultaneously carried the putative regulatory genes. Deletion of tosR alleviates tosA repression. The tos promoter was localized upstream of tosR using transcriptional fusions of putative promoter regions with lacZ. TosR binds to this region, affecting a gel shift. A 100-bp fragment 220 to 319 bp upstream of tosR inhibits binding, suggesting localization of the TosR binding site. TosEF, on the other hand, downmodulate motility when overexpressed by preventing the expression of fliC, encoding flagellin. Deletion of tosEF increased motility. Thus, we present an additional example of the reciprocal control of adherence and motility. U rinary tract infections (UTIs) are the second most common bacterial infection in humans (1). UTIs can be classified as complicated or uncomplicated infections. Uncomplicated UTIs, occurring in otherwise healthy individuals, are self-limited infections of the bladder, referred to as cystitis (2-4). However, upon bacterial ascension into the kidney, a more serious infection referred to as pyelonephritis can develop (2, 4). Pyelonephritis, in turn, can lead to the development of bacteremia and sometimes fatal urosepsis (5, 6).UTIs normally occur when uropathogens that colonize the intestine alongside commensal organisms gain access to the periurethral area and then ascend to the urinary bladder (7,8). A heterogeneous subset of extraintestinal pathogenic Escherichia coli (ExPEC) strains, referred to as uropathogenic E. coli (UPEC), causes the overwhelming majority of uncomplicated UTIs (4). UPEC strains carry a battery of virulence factors, including adhesins, toxins, and iron acquisition systems, which promote uropathogenesis (9, 10). However, no core set of virulence factors has been identified. Instead, any given UPEC strain appears to use various virulence factors from these three classes of virulence determinants to colonize the urinary tract (11,12). This thesis requires that we consider established, newly discovered, and putative virule...

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TheSalmonella entericagiant adhesin SiiE binds to polarized epithelial cells in a lectin-like manner

Cited by 37 publications

References 40 publications

Salmonella enterica Invasion of Polarized Epithelial Cells Is a Highly Cooperative Effort

Salmonella enterica Invasion of Polarized Epithelial Cells Is a Highly Cooperative Effort

Structural and functional dissection reveals distinct roles of Ca2+-binding sites in the giant adhesin SiiE of Salmonella enterica

A Conserved PapB Family Member, TosR, Regulates Expression of the Uropathogenic Escherichia coli RTX Nonfimbrial Adhesin TosA while Conserved LuxR Family Members TosE and TosF Suppress Motility

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