Molecular mechanisms and biological role of<i>Campylobacter jejuni</i>attachment to host cells

Rubinchik, Sona; Seddon, Alan M.; Karlyshev, Andrey V.

doi:10.1556/eujmi.2.2012.1.6

Cited by 39 publications

(36 citation statements)

References 75 publications

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“…In susceptible hosts, attachment by C. jejuni initiates an array of pathogenic events, including intracellular invasion, translocation across the intestinal barrier, interaction with immune cells and induction of damage to host tissues. Of these, three, JlpA, CadF and FlpA, have known host cell receptors [88] (Fig. Unlike flagella, pili are not considered to be essential for C. jejuni attachment [86,87].…”

Section: Attachmentmentioning

confidence: 99%

“…Flagella play a critical role in the attachment process for several members of the Campylobacter genus, including C. jejuni. 67.1), whereas for a further nine C. jejuni proteins implicated in mediating adhesion to host cell surfaces the host receptors remain unknown [88] ( Fig. Several adhesins in C. jejuni have been shown to mediate attachment to host cells [88].…”

Section: Attachmentmentioning

confidence: 99%

“…In addition to flagellin, JlpA, CadF and FlpA, nine other proteins of C. jejuni have been implicated to have a role in bacterial attachment, namely PEB1, PEB3, PEB4, CapA, CapB, Cj1349, Cj0091, TlyA and P95 [88] ( Fig. 67.1).…”

Section: Relationships Between Adhesinsmentioning

confidence: 99%

“…67.1). The host receptors for these have not been determined and their roles as adhesins have been reviewed elegantly by Rubinchik and colleagues [88]. Pei and colleagues have reported that at least 50% of patients infected with C. jejuni or C. coli exhibit seroconversion to the C. jejuni PEB1, PEB3 and PEB4 proteins [139].…”

Section: Relationships Between Adhesinsmentioning

confidence: 99%

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Campylobacter

Kaakoush

Mitchell

Man

2015

Molecular Medical Microbiology

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Section: Attachmentmentioning

confidence: 99%

Section: Attachmentmentioning

confidence: 99%

Section: Relationships Between Adhesinsmentioning

confidence: 99%

Section: Relationships Between Adhesinsmentioning

confidence: 99%

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Campylobacter

Kaakoush

Mitchell

Man

2015

Molecular Medical Microbiology

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“…Moreover, the OM is an essential permeability barrier (thus affecting antibiotic sensitivity) and a key player in nutrient acquisition, natural competence and biofilm formation. Most of these functions are protein-mediated; in C. jejuni the importance of a number of OM proteins (OMPs) have been determined, including porins such as the Major Outer Membrane Porin (MOMP; PorA), the fibronectin binding protein CadF, other adhesins such as PEB1a, CjaA and JlpA and the autotransporter CapA (Rubinchik et al, 2012; Mahdavi et al, 2014; Wu et al, 2016). Highly antigenic OMPs have already been proposed as vaccine candidates, in both chickens and humans (Tribble et al, 2008).…”

Section: Introductionmentioning

confidence: 99%

The Periplasmic Chaperone Network of Campylobacter jejuni: Evidence that SalC (Cj1289) and PpiD (Cj0694) Are Involved in Maintaining Outer Membrane Integrity

2017

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The outer membrane (OM) of Gram-negative pathogenic bacteria is a key structure in host–pathogen interactions that contains a plethora of proteins, performing a range of functions including adhesion, nutrient uptake, export of effectors and interaction with innate and adaptive components of the immune system. In addition, the OM can exclude drugs and thus contribute to antimicrobial resistance. The OM of the food-borne pathogen Campylobacter jejuni contains porins, adhesins and other virulence factors that must be specifically localized to this membrane, but the protein sorting mechanisms involved are only partially understood. In particular, chaperones are required to ferry OM proteins across the periplasm after they emerge from the Sec translocation system. The SurA-related chaperone PEB4 (Cj0596) is the only protein with a proven role in OM biogenesis and integrity in C. jejuni. In this work, we have constructed a set of isogenic deletion mutants in genes encoding both known and predicted chaperones (cj0596, cj0694, cj1069, cj1228c, and cj1289) using NCTC 11168H as the parental strain. These mutants were characterized using a range of assays to determine effects on growth, agglutination, biofilm formation, membrane permeability and hydrophobicity. We focused on Cj1289 and Cj0694, which our previous work suggested possessed both chaperone and peptidyl-proyl cis/trans isomerase (PPIase) domains. Mutants in either cj1289 or cj0694 showed growth defects, increased motility, agglutination and biofilm formation and severe OM permeability defects as measured by a lysozyme accessibility assay, that were comparable to those exhibited by the isogenic peb4 mutant. 2D-gel comparisons showed a general decrease in OM proteins in these mutants. We heterologously overproduced and purified Cj0694 and obtained evidence that this protein was an active PPIase, as judged by its acceleration of the refolding rate of reduced and alkylated ribonuclease T1 and that it also possessed holdase-type chaperone activity. Cj0694 is most similar to the PpiD class of chaperones but is unusual in possessing PPIase activity. Taken together, our data show that in addition to PEB4, Cj1289 (SalC; SurA-like chaperone) and Cj0694 (PpiD) are also key proteins involved in OM biogenesis and integrity in C. jejuni.

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Bacterial Infections of the Small and Large Intestine

Bernard

Nicholson

2021

Textbook of Pediatric Gastroenterology, Hepatology and Nutrition

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Molecular mechanisms and biological role ofCampylobacter jejuniattachment to host cells

Cited by 39 publications

References 75 publications

Campylobacter

Campylobacter

The Periplasmic Chaperone Network of Campylobacter jejuni: Evidence that SalC (Cj1289) and PpiD (Cj0694) Are Involved in Maintaining Outer Membrane Integrity

Bacterial Infections of the Small and Large Intestine

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