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Istituto di scienza dell'alimentazione

Torna all'elenco Contributi in rivista anno 2006

Contributo in rivista

Tipo: Articolo in rivista

Titolo: Bovine lactoferrin peptidic fragments involved in inhibition of Echovirus 6 in vitro infection.

Anno di pubblicazione: 2006

Formato: Elettronico Cartaceo

Autori: Pietrantoni A; Ammendolia MG; Tinari A; Siciliano R; Valenti P; Superti F.

Affiliazioni autori: Department of Technology and Health, National Institute of Health, Viale Regina Elena, 299, 00161 Rome, Italy Institute of Food Science and Technology, CNR, Avellino, Italy Department of Experimental Medicine, II University of Naples, Naples, Italy

Autori CNR:


Lingua: inglese

Abstract: Bovine lactoferrin is a multifunctional glycoprotein folded in two symmetric globular lobes (N- and C-lobes), each being able to bind one ferric ion. We have previously demonstrated that this protein is able to prevent echovirus-induced apoptosis. In the present study, we have investigated both the role of tryptic fragments of bovine lactoferrin and the mechanism of lactoferrin effect on echovirus infection. Results obtained showed that bovine lactoferrin inhibits echovirus-induced cytopathic effect and antigen synthesis in a dose-dependent manner and that this protein is able to prevent viral replication when added not only during the entire cycle of infection but also before, during or after the viral adsorption step. The N-terminal cationic peptide was sufficient to prevent viral binding. Our data suggest that lactoferrin inhibition of echovirus attachment to cell receptors could be mediated by the cluster of positive charges at its N-terminus (lactoferricin).

Lingua abstract: inglese

Pagine da: 98

Pagine a: 106

Pagine totali: 9


Antiviral research Elsevier/North-Holland,
Paese di pubblicazione: Paesi Bassi
Lingua: inglese
ISSN: 0166-3542

Numero volume: 69

DOI: 10.1016/j.antiviral.2005.10.006

Referee: Sė: Internazionale

Indicizzato da:

  • ISI Web of Science (WOS) [000235418100006]
  • PubMed [16386316]
  • Scopus [2-s2.0-31444434715]

Strutture CNR:


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