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

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).

• Authors: Agostina Pietrantoni, Maria Grazia Ammendolia, Antonella Tinari, Rosa Siciliano, Piera Valenti, Fabiana Superti
• Journal: Antiviral research (Antiviral Res) Vol. 69 Issue 2 Pg. 98-106 (Feb 2006) ISSN: 0166-3542 [Print] Netherlands
• PMID: 16386316 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• Antigens, Viral
• Antiviral Agents
• Peptide Fragments
• Lactoferrin

Topics

• Animals
• Antigens, Viral (biosynthesis)
• Antiviral Agents (chemistry, pharmacology)
• Cattle
• Cell Line
• Cytopathogenic Effect, Viral (drug effects)
• Echovirus 6, Human (drug effects, pathogenicity)
• Lactoferrin (chemistry, pharmacology)
• Microscopy, Electron, Transmission
• Peptide Fragments (chemistry, pharmacology)