http://www.cnr.it/ontology/cnr/individuo/prodotto/ID45892
Surface displaced alfa-enolase of Lactobacillus plantarum is a fibronectin binding protein. (Articolo in rivista)
- Type
- Label
- Surface displaced alfa-enolase of Lactobacillus plantarum is a fibronectin binding protein. (Articolo in rivista) (literal)
- Anno
- 2009-01-01T00:00:00+01:00 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
- 10.1186/1475-2859-8-14 (literal)
- Alternative label
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
- Castaldo C; Vastano V; Siciliano RA; Candela M; Vici M; Muscariello L; Marasco R; Sacco M. (literal)
- Pagina inizio
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#url
- http://www.microbialcellfactories.com/content/8/1/14 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
- Rivista
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#pagineTotali
- Note
- Scopu (literal)
- ISI Web of Science (WOS) (literal)
- PubMe (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
- Dipartimento di Scienze Ambientali, Seconda Università di Napoli, via Vivaldi 43, 81100 Caserta, Italy
Centro di Spettrometria di Massa Proteomica e Biomolecolare, Istituto di Scienze dell'Alimentazione, CNR, Avellino, Italy, Dipartimento di Scienze Farmaceutiche, Università di Bologna, via Belmeloro 6, 40126 Bologna, Italy,
Dipartimento di Patologia Sperimentale, Università di Bologna, via S. Giacomo 14, 40126 Bologna, Italy and
Dipartimento di Scienze della Vita, Seconda Università di Napoli, via Vivaldi 43, 81100 Caserta, Italy (literal)
- Titolo
- Surface displaced alfa-enolase of Lactobacillus plantarum is a fibronectin binding protein. (literal)
- 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.
Results: We show the identification of a Lactobacillus plantarum LM3 cell surface protein (48 kDa), which
specifically binds to human fibronectin (Fn), an extracellular matrix protein. By means of mass spectrometric
analysis this protein was identified as the product of the L. plantarum enoA1 gene, coding the EnoA1 alfa-enolase.
Surface localization of EnoA1 was proved by immune electron microscopy. In the mutant strain LM3-CC1,
carrying the enoA1 null mutation, the 48 kDa adhesin was not anymore detectable neither by anti-enolase
Western blot nor by Fn-overlay immunoblotting assay. Moreover, by an adhesion assay we show that LM3-CC1
cells bind to fibronectin-coated surfaces less efficiently than wild type cells, thus demonstrating the significance of
the surface displaced EnoA1 protein for the L. plantarum LM3 adhesion to fibronectin.
Conclusion: Adhesion to host tissues represents a crucial early step in the colonization process of either
pathogens or commensal bacteria. We demonstrated the involvement of the L. plantarum Eno A1 alfa-enolase in
Fn-binding, by studying LM3 and LM3-CC1 surface proteins. Isolation of LM3-CC1 strain was possible for the
presence of expressed enoA2 gene in the L. plantarum genome, giving the possibility, for the first time to our
knowledge, to quantitatively compare adhesion of wild type and mutant strain, and to assess doubtless the role
of L. plantarum Eno A1 as a fibronectin binding protein. (literal)
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