FimH adhesin from host unrestricted Salmonella Enteritidis binds to different glycoprotein ligands expressed by enterocytes from sheep, pig and cattle than FimH adhesins from host restricted Salmonella Abortus-ovis, Salmonella Choleraesuis and Salmonella Dublin

Grzymajło, Krzysztof; Ugorski, Maciej; Kolenda, Rafał; Kędzierska, Anna; Kuźmińska-Bajor, Marta; Wieliczko, Alina

doi:10.1016/j.vetmic.2013.07.004

Cited by 23 publications

(33 citation statements)

References 24 publications

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“…There are several molecular mechanisms, including bacterial adherence, replication in host cells, species-specific toxins or metal acquisition involved in host specificity of Salmonella (reviewed in Baumler and Fang, 2013). It was previously shown that FimH adhesin single nucleotide polymorphisms (SNPs) impact adhesion properties of E. coli (Sokurenko et al, 1994) and Salmonella (Boddicker et al, 2002; Grzymajlo et al, 2010), as well as Salmonella host specificity (Boddicker et al, 2002; Grzymajlo et al, 2010, 2013; Kisiela et al, 2012; Yue et al, 2015). Furthermore, host-adapted S .…”

Section: Discussionmentioning

confidence: 99%

“…Recombinant FimH adhesins were obtained as described in our previous paper (Grzymajlo et al, 2013) and named CFimH (active FimH variant from S . Choleraesuis), EFimH (active FimH variant from S .…”

Section: Methodsmentioning

confidence: 99%

“…Established enterocyte cell lines express intestinal membrane components and, therefore, can act as a suitable model for host-pathogen interactions in the initial phases of bacterial pathogenesis (Brosnahan and Brown, 2012). In our previous study (Grzymajlo et al, 2013), we found that the IPEC-J2 cell line (Schierack et al, 2006), a widely described porcine intestinal cell model, expresses a protein specifically recognized by S . Choleraesuis FimH.…”

Section: Introductionmentioning

confidence: 96%

“…Our previous study showed that FimH adhesins from host-adapted serovars - Salmonella Choleraesuis, Salmonella Abortusovis and Salmonella Dublin - bind to membrane proteins of approximately 55 kDa expressed by pig, sheep, and cattle enterocytes, respectively. In contrast, FimH protein from host-unrestricted Salmonella Enteritidis binds to glycoproteins of approximately 130 kDa present on the surface of these cells (Grzymajlo et al, 2013). Therefore, our data suggest the existence of specific receptors expressed by host cells, which are selectively recognized by allelic variants of FimH adhesins expressed by Salmonella serovars with different host specificities.…”

Section: Introductionmentioning

confidence: 99%

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The Novel Type 1 Fimbriae FimH Receptor Calreticulin Plays a Role in Salmonella Host Specificity

Grzymajło

Ugorski

Suchański

et al. 2017

Front. Cell. Infect. Microbiol.

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It was suggested that minor differences in the structure of FimH are most likely associated with differences in its adhesion specificities and may determine the tropism of various Salmonella serovars to different species and tissues. We have recently shown that FimH adhesins from host-adapted serovars, e.g., Salmonella Choleraesuis (SCh), bind to other glycoprotein receptors compared to FimH from host-unrestricted Salmonella Enteritidis (SE). Here we identify porcine calreticulin expressed by swine intestinal cells as a host-specific receptor for SCh FimH adhesin, suggesting that such an interaction may contribute to SCh host specificity. Calreticulin was identified by 2D electrophoresis and mass spectrometry as a glycoprotein that was bound specifically by recombinant SCh FimH protein, but not by FimH from SE. The functionality of calreticulin as a specific receptor of SCh FimH adhesin was further confirmed by adhesion and invasion of mutated strains of SCh carrying different variants of FimH proteins to IPEC-J2 cells with overexpression and silenced expression of calreticulin. It was found that SCh carrying the active variant of FimH adhered and invaded IPEC-J2 cells with calreticulin overexpression at significantly higher numbers than those of SCh expressing the non-active variant or SE variant of FimH. Moreover, binding of SCh carrying the active variant of FimH to IPEC-J2 with silenced calreticulin expression was significantly weaker. Furthermore, we observed that SCh infection induces translocation of calreticulin to cell membrane. All of the aforementioned results lead to the general conclusion that Salmonella host specificity requires not only special mechanisms and proteins expressed by the pathogen but also specifically recognized receptors expressed by a specific host.

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Section: Discussionmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 96%

Section: Introductionmentioning

confidence: 99%

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The Novel Type 1 Fimbriae FimH Receptor Calreticulin Plays a Role in Salmonella Host Specificity

Grzymajło

Ugorski

Suchański

et al. 2017

Front. Cell. Infect. Microbiol.

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“…Its structure forms an extracellular appendage whose top protein, FimH, has been demonstrated to bind mannosyl residues strongly (Bouckaert et al, 2005;Wellens et al, 2008;Korea, Ghigo & Beloin, 2011). Type 1 fimbriae have been implicated in the specific adhesion of various enterobacteria to human epithelial cells (Grzymajło et al, 2013). They were also found associated with membranous cells, a class of cells found in Peyer's patches in the gut epithelium, which are linked with antigen transportation through the specific involvement of glycoprotein 2, a highly N-glycosylated protein (Ohno & Hase, 2010).…”

Section: Recognition Of Eukaryotic Mannosides By Bacteriamentioning

confidence: 99%

Mannoside recognition and degradation by bacteria

et al. 2016

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Mannosides constitute a vast group of glycans widely distributed in nature. Produced by almost all organisms, these carbohydrates are involved in numerous cellular processes, such as cell structuration, protein maturation and signalling, mediation of protein-protein interactions and cell recognition. The ubiquitous presence of mannosides in the environment means they are a reliable source of carbon and energy for bacteria, which have developed complex strategies to harvest them. This review focuses on the various mannosides that can be found in nature and details their structure. It underlines their involvement in cellular interactions and finally describes the latest discoveries regarding the catalytic machinery and metabolic pathways that bacteria have developed to metabolize them.

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Genomic Diversity in Salmonella enterica

Wain

O’Grady

2017

Applied Genomics of Foodborne Pathogens

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Salmonella enterica is a bacterial species which contains diversity within the limits of a single species ancestry. Selection by different habitats, represented by the extraordinary number of host species colonised by S. enterica, and the need to successfully transmit through water, soil, or fomites (from host to host) has driven this diversity. An understanding of the impact of this diversity needs to drive the naming of isolates which should be clinically and biologically relevant in terms of niche occupation as well as in terms of ancestry; all we need is an accurate sequence of the entire genome and a comprehensive understanding of the biology of the variation seen. Currently serotype is the working unit of classification but the variation seen within each serotype is itself very variable and so not all serotypes are equal. Here we describe the current genomic data from several common serotypes and discuss the biology behind the different levels of variation

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FimH adhesin from host unrestricted Salmonella Enteritidis binds to different glycoprotein ligands expressed by enterocytes from sheep, pig and cattle than FimH adhesins from host restricted Salmonella Abortus-ovis, Salmonella Choleraesuis and Salmonella Dublin

Cited by 23 publications

References 24 publications

The Novel Type 1 Fimbriae FimH Receptor Calreticulin Plays a Role in Salmonella Host Specificity

The Novel Type 1 Fimbriae FimH Receptor Calreticulin Plays a Role in Salmonella Host Specificity

Mannoside recognition and degradation by bacteria

Genomic Diversity in Salmonella enterica

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