Surface displaced alfa-enolase of Lactobacillus plantarum is a fibronectin binding protein

Abstract

Background: Lactic acid bacteria of the genus Lactobacillus and Bifidobacterium are one of the most important health promoting groups of the human intestinal microbiota. Their protective role within the gut consists in out competing invading pathogens for ecological niches and metabolic substrates. Among the features necessary to provide health benefits, commensal microorganisms must have the ability to adhere to human intestinal cells and consequently to colonize the gut. Studies on mechanisms mediating adhesion of lactobacilli to human intestinal cells showed that factors involved in the interaction vary mostly among different species and strains, mainly regarding interaction between bacterial adhesins and extracellular matrix or mucus proteins. We have investigated the adhesive properties of Lactobacillus plantarum, a member of the human microbiota of healthy individuals.

Characterization of pyruvate dehydrogenase subunit B and enolase as plasminogen-binding proteins in Mycoplasma pneumoniae

“…, C. albicans (Jong et al, 2003), Lactobacillus plantarum (Castaldo et al, 2009), Paracoccidioides brasiliensis (Donofrio et al, 2009), Staphylococcus aureus (Carneiro et al, 2004), S. pneumoniae (Bergmann et al, 2001) and Trichomonas vaginalis (Mundodi et al, 2008). In most cases, enolases interact with plasminogen but binding to fibronectin and laminin has also been reported (Carneiro et al, 2004;Castaldo et al, 2009;Donofrio et al, 2009). The M. pneumoniae enolase shows typical putative plasminogen-binding sites, such as lysine in the C terminus, 448 FKNIK 452 , and a lysine-rich internal motif, 268 KRYVFKKGIKAKILDEK 284 (Bergmann et al, 2003;Derbise et al, 2004;Yavlovich et al, 2007).…”

“…Besides GAPDH, enolase is one of most frequent members of the class of surface-localized glycolytic enzymes, as described in phylogenetically different species such as Aeromonas hydrophila (Sha et al, 2009), Bacillus anthracis (Agarwal et al, 2008), Borrelia burgdorferi (Nogueira et al, 2012), Bifidobacterium sp. , C. albicans (Jong et al, 2003), Lactobacillus plantarum (Castaldo et al, 2009), Paracoccidioides brasiliensis (Donofrio et al, 2009), Staphylococcus aureus (Carneiro et al, 2004), S. pneumoniae (Bergmann et al, 2001) and Trichomonas vaginalis (Mundodi et al, 2008). In most cases, enolases interact with plasminogen but binding to fibronectin and laminin has also been reported (Carneiro et al, 2004;Castaldo et al, 2009;Donofrio et al, 2009).…”

Bacterial Virulence in the Moonlight: Multitasking Bacterial Moonlighting Proteins Are Virulence Determinants in Infectious Disease

“…The binding of group A streptococcal GAPDH to fibronectin has already been described (137). Lactobacillus plantarum has a cell surface enolase which binds fibronectin (37). Fibronectin has a complex domain structure, with different parts of the protein binding to different host components including heparin, collagen, gelatin, fibulin, etc.…”

Extracellular proteins secreted by probiotic bacteria as mediators of effects that promote mucosa–bacteria interactions

“…Finally, several glycolytic, housekeeping and ribosomal proteins are often found on the surface of bacteria (Jeffery, 2003). It is still unknown how these intracellular proteins can span the cytoplasmic membrane and reach the cell surface, although it is assumed that, once surface-exposed, these proteins could develop other functions, serving, for example, as adhesins Castaldo et al, 2009;Hurmalainen et al, 2007;Kinoshita et al, 2008a, b;Ramiah et al, 2008). Because of their property of having different functions, depending on the subcellular localization, these proteins are termed 'moonlighting' proteins (Jeffery, 2003).…”