Abstract

ABSTRACT Due to the global spread of multidrug resistant pathogenic bacteria, alternative approaches in combating infectious diseases are required. One such approach is the use of probiotics. Lactobacillus fermentum 3872 is a promising probiotic bacterium producing a range of antimicrobial compounds, such as hydrogen peroxide and lactic acid. In addition, previous studies involving genome sequencing and analysis of L. fermentum 3872 allowed the identification of a gene encoding a cell surface protein referred to as collagen binding protein (CBP) (not found in other strains of the species, according to the GenBank database), consisting of a C-terminal cell wall anchor domain (LPXT), multiple repeats of ‘B domains' that form stalks presenting an “A domain” required for adhesion. In this study, we found that the CBP of L. fermentum 3872 binds to collagen I present on the surface of the epithelial cells lining the gastrointestinal tract. Moreover, we found that this host receptor is also used for attachment by the major gastrointestinal pathogen, Campylobacter jejuni. Furthermore, we identified an adhesin involved in such interaction and demonstrated that both L. fermentum 3872 and its CBP can inhibit binding of this pathogen to collagen I. Combined with the observation that C. jejuni growth is affected in the acidic environment produced by L. fermentum 3872, the finding provides a good basis for further investigation of this strain as a potential tool for fighting Campylobacter infections.

Highlights

  • Campylobacter jejuni is an enteric pathogen and one of the most common causes of gastroenteritis in humans with symptoms such as abdominal pains, watery or bloody diarrhoea, and fever 1

  • Expression of the L. fermentum 3872 CPB in E. coli as a His-tagged fusion protein allowed its purification as a stable product of an expected size (111 kDa predicted, 115 kDa estimated from a gel, Fig. S1)

  • Since C. jejuni strains 11168H and [81-176] were able to bind to collagen I in a concentration-dependent manner (Fig. 2), we aimed to establish if these bacteria compete with the purified collagen binding protein (CBP) for the binding sites

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Summary

Introduction

Campylobacter jejuni is an enteric pathogen and one of the most common causes of gastroenteritis in humans with symptoms such as abdominal pains, watery or bloody diarrhoea, and fever 1. C. jejuni infections can lead to a neurodegenerative disease such as Guillain-Barre syndrome 2. C. jejuni infections are often caused by poor hygiene standards, consumption of undercooked meat, contaminated water and/or milk 3. Fatalities associated with C. jejuni infections are uncommon, can occur among immunologically naïve patients 4. C. jejuni infections are an economic burden leading to many hospitalisations/primary care visits 5. There has been a rise in antimicrobial resistant forms of C. jejuni caused by the misuse of antimicrobials 6. C. jejuni has been placed on a list of antibiotic-resistant priority pathogens by the world health organisation (WHO) to promote research and development in novel antimicrobials 7. Due to the appearance of multidrug resistant forms of these bacteria, there is growing interest in using alternative approaches to combat C. jejuni infections

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