<i>Campylobacter jejuni</i>
            FlpA Binds Fibronectin and Is Required for Maximal Host Cell Adherence

Konkel, Michael E.; Larson, Carl L.; Flanagan, Rebecca C.

doi:10.1128/jb.00969-09

Cited by 103 publications

(113 citation statements)

References 29 publications

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“…Putative adhesion factors have been identified, e.g. the fibronectinbinding proteins CadF and FlpA (Konkel et al, 1997(Konkel et al, , 2010, the autotransporter CapA, and a surface-exposed lipoprotein, JIpA (Jin et al, 2001). In addition, the sialylated lipooligosaccharide outer core of C. jejuni has been demonstrated to be an important factor for the invasion of epithelial cells (Guerry et al, 2000;Louwen et al, 2008).…”

Section: Introductionmentioning

confidence: 99%

Campylobacter jejuni proteins Cj0952c and Cj0951c affect chemotactic behaviour towards formic acid and are important for invasion of host cells

et al. 2010

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Campylobacter jejuni, an important food-borne bacterial pathogen in industrialized countries and in the developing world, is one of the major causes of bacterial diarrhoea. To identify genes which are important for the invasion of host cells by the pathogen, we screened altogether 660 clones of a transposon-generated mutant library based on the clinical C. jejuni isolate B2. Thereby, we identified a clone with a transposon insertion in gene cj0952c. As in the well-characterized C. jejuni strain NCTC 11168, the corresponding protein together with the gene product of the adjacent gene cj0951c consists of two transmembrane domains, a HAMP domain and a putative MCP domain, which together are thought to act as a chemoreceptor, designated Tlp7. In this report we show that genes cj0952c and cj0951c (i) are important for the host cell invasion of the pathogen, (ii) are not translated as one protein in C. jejuni isolate B2, contradicting the idea of a postulated read-through mechanism, (iii) affect the motility of C. jejuni, (iv) alter the chemotactic behaviour of the pathogen towards formic acid, and (v) are not related to the utilization of formic acid by formate dehydrogenase.

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Section: Introductionmentioning

confidence: 99%

Campylobacter jejuni proteins Cj0952c and Cj0951c affect chemotactic behaviour towards formic acid and are important for invasion of host cells

et al. 2010

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“…Host cell receptors have been identified only for outer membrane proteins CadF and FlpA specific to fibronectin (Fn) [16][17][18][19] and JlpA, specific to heat shock protein 90 [20].…”

Section: Confirmed Protein Adhesinsmentioning

confidence: 99%

“…Fn-binding protein FlpA contains Fn type III domains [17,18]. Disruption of the flpA gene impairs bacterial ability to adhere to chicken LMH hepatocellular carcinoma epithelial cells and to human INT 407 cells, and reduces bacterial ability to colonise chickens [17].…”

Section: Confirmed Protein Adhesinsmentioning

confidence: 99%

Molecular mechanisms and biological role ofCampylobacter jejuniattachment to host cells

Rubinchik

Seddon

Karlyshev

2012

European Journal of Microbiology and Immunology

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“…Due to the low number of recognized bacterial FNIII domains at that time, and phylogenetic analysis placing them separate from the eukaryotic domains, it was suggested that prokaryotes had acquired FNIII domains from eukaryotes [7]. All initially identified prokaryotic FNIII domains were associated with carbohydrate acting enzymes, but more recently these domains have also been identified in fibronectin binding proteins and multiple other prokaryotic protein types [8][9][10]. Our database searches showed that about 33% of all FNIII containing proteins included in SMART database (15125) [10] are from bacteria.…”

Section: Introductionmentioning

confidence: 99%

“…So far no reciprocal protein-protein interactions have been reported to exist between bacterial FNIII domains, although an interaction has been suggested to exist between fibronectin binding proteins FNIII domains and eukaryotic fibronectin [9]. Characterization of different carbohydrate acting enzymes resulted in three suggestions for the role of their FNIII domains: as stable linker [14], carbohydrate surface disruption domain [15] and CBM [16].…”

Section: Introductionmentioning

confidence: 99%

The evolutionary origin and possible functional roles of FNIII domains in two Microbacterium aurum B8.A granular starch degrading enzymes, and in other carbohydrate acting enzymes

Valk

Kaaij

Dijkhuizen

2017

Amylase

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Fibronectin type III (FNIII) domains were first identified in the eukaryotic plasma protein fibronectin, where they act as structural spacers or enable protein-protein interactions. Recently we characterized two large and multi-domain amylases in Microbacterium aurum B8.A that both carry multiple FNIII and carbohydrate binding modules (CBMs). The role of (multiple) FNIII domains in such carbohydrate acting enzymes is currently unclear. Four hypothetical functions are considered here: a substrate surface disruption domain, a carbohydrate binding module, as a stable linker, or enabling protein-protein interactions. We performed a phylogenetic analysis of all FNIII domains identified in proteins listed in the CAZy database. These data clearly show that the FNIII domains in eukaryotic and archaeal CAZy proteins are of bacterial origin and also provides examples of interkingdom gene transfer from Bacteria to Archaea and Eucarya. FNIII domains occur in a wide variety of CAZy enzymes acting on many different substrates, suggesting that they have a non-specific role in these proteins. While CBM domains are mostly found at protein termini, FNIII domains are commonly located between other protein domains. FNIII domains in carbohydrate acting enzymes thus may function mainly as stable linkers to allow optimal positioning and/or flexibility of the catalytic domain and other domains, such as CBM.

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Campylobacter jejuni FlpA Binds Fibronectin and Is Required for Maximal Host Cell Adherence

Cited by 103 publications

References 29 publications

Campylobacter jejuni proteins Cj0952c and Cj0951c affect chemotactic behaviour towards formic acid and are important for invasion of host cells

Campylobacter jejuni proteins Cj0952c and Cj0951c affect chemotactic behaviour towards formic acid and are important for invasion of host cells

Molecular mechanisms and biological role ofCampylobacter jejuniattachment to host cells

The evolutionary origin and possible functional roles of FNIII domains in two Microbacterium aurum B8.A granular starch degrading enzymes, and in other carbohydrate acting enzymes

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