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Istituto di scienza dell'alimentazione

Torna all'elenco Contributi in rivista anno 2013

Contributo in rivista

Tipo: Articolo in rivista

Titolo: Identification of binding sites of Lactobacillus plantarum enolase involved in the interaction with human plasminogen.

Anno di pubblicazione: 2013

Formato: Elettronico Cartaceo

Autori: Vastano V, Capri U, Candela M, Siciliano RA, Russo L, Renda M, Sacco M.

Affiliazioni autori: Dipartimento di Scienze Ambientali, Seconda UniversitÓ di Napoli, Caserta, Italy Dipartimento di Scienze Farmaceutiche, UniversitÓ di Bologna, Bologna, Italy Centro di Spettrometria di Massa Proteomica e Biomolecolare, Istituto di Scienze dell'Alimentazione, CNR, Avellino, Italy Department of NMR-based Structural Biology, Max-Planck Institute for Biophysical Chemistry, G÷ttingen, Germany

Autori CNR:

  • ROSA ANNA SICILIANO

Lingua: inglese

Abstract: The enolase EnoA1 of Lactobacillus plantarum is here shown to interact with human plasminogen (Plg). By sequence alignment of EnoA1 with Streptococcus pneumoniae and Bifidobacterium lactis enolases, we identified BS1 and BS2 Plg-binding sites. A structure prediction of EnoA1 showed lysine residues in position 255 (BS2), and 422 (BS1) exposed on protein surface. A lysine residue in position 259 was as well identified as surface-exposed amino acid. The enoA1 gene was site directed-mutagenized to generate four mutated proteins, carrying K255A, K259A, K422A and K259A/K422A substitutions. The functional role of these lysine residues was assessed evaluating specific Plg-binding activity of the mutated proteins. While the binding activity of the mutated proteins was drastically reduced, the residual enzymatic activity was more than 50% of EnoA1. Our results show that L. plantarum EnoA1 exhibits the Plg-BS1, and the Plg-BS2 extending up to the lysine residue in position 259, therefore consisting of 12-aa residues instead of 9-aa residues described in S. pneumoniae. A test performed on whole cells of L. plantarum, demonstrated that after inducing conversion of the cell-bound plasminogen to plasmin, this was released into the medium, unlike the mechanism reported for most pathogens, that retained plasmin bound to the cell surface.

Lingua abstract: inglese

Pagine da: 65

Pagine a: 72

Pagine totali: 8

Rivista:

Microbiological research Elsevier.
Paese di pubblicazione: Germania
Lingua: inglese
ISSN: 0944-5013

Numero volume: 168

DOI: 10.1016/j.micres.2012.10.001

Referee: Sý: Internazionale

Indicizzato da: PubMed [PMID: 23103380]

Parole chiave:

  • Lactobacillus plantarum; Adhesins; Enolase; Plasminogen; Probiotics

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