Next Article in Journal
Mouse Models Reveal Role of T-Cytotoxic and T-Reg Cells in Immune Response to Influenza: Implications for Vaccine Design
Previous Article in Journal
The Robust Self-Assembling Tubular Nanostructures Formed by gp053 from Phage vB_EcoM_FV3
Article

Bovine Lactoferrin Prevents Influenza A Virus Infection by Interfering with the Fusogenic Function of Viral Hemagglutinin

1
National Centre for Innovative Technologies in Public Health, National Institute of Health, Viale Regina Elena 299, 00161 Rome, Italy
2
Department of Pharmacy, University “G. d’Annunzio”, Via dei Vestini 31, 66100 Chieti, Italy
3
Core Facilities, National Institute of Health, Viale Regina Elena 299, 00161 Rome, Italy
*
Author to whom correspondence should be addressed.
Viruses 2019, 11(1), 51; https://doi.org/10.3390/v11010051
Received: 6 December 2018 / Revised: 7 January 2019 / Accepted: 8 January 2019 / Published: 11 January 2019
(This article belongs to the Section Animal Viruses)
Bovine lactoferrin (bLf) is an iron-binding glycoprotein folded in two symmetric globular lobes (N- and C-lobes) with potent antimicrobial and immunomodulatory activities. Recently, we have shown that bLf, and in particular its C-lobe, interacts with influenza A virus hemagglutinin and prevents infection by different H1 and H3 viral subtypes. Influenza virus hemagglutinin (HA), and in particular its highly conserved fusion peptide involved in the low-pH-mediated fusion process, plays a significant role in the early steps of viral infection and represents an attractive target for the development of anti-influenza drugs. In the present research, we further investigated the influence of low pH on the interactions between bLf and influenza A H1N1 virus by different techniques, such as enzyme-linked immunosorbent assay, electron microscopy, hemolysis inhibition assay, and time course assay. Our results demonstrate that lactoferrin interaction with influenza hemagglutinin at low pH induces alterations that stabilize the conformation of the hemagglutinin, resulting in the inhibition of the fusion peptide activity. Taken together, our data allowed to better characterize the HA-specific inhibiting activity of bLf and to confirm HA as a good target for drug development. View Full-Text
Keywords: influenza virus; fusion peptide; lactoferrin; antiviral agents influenza virus; fusion peptide; lactoferrin; antiviral agents
Show Figures

Figure 1

MDPI and ACS Style

Superti, F.; Agamennone, M.; Pietrantoni, A.; Ammendolia, M.G. Bovine Lactoferrin Prevents Influenza A Virus Infection by Interfering with the Fusogenic Function of Viral Hemagglutinin. Viruses 2019, 11, 51. https://doi.org/10.3390/v11010051

AMA Style

Superti F, Agamennone M, Pietrantoni A, Ammendolia MG. Bovine Lactoferrin Prevents Influenza A Virus Infection by Interfering with the Fusogenic Function of Viral Hemagglutinin. Viruses. 2019; 11(1):51. https://doi.org/10.3390/v11010051

Chicago/Turabian Style

Superti, Fabiana, Mariangela Agamennone, Agostina Pietrantoni, and Maria G. Ammendolia 2019. "Bovine Lactoferrin Prevents Influenza A Virus Infection by Interfering with the Fusogenic Function of Viral Hemagglutinin" Viruses 11, no. 1: 51. https://doi.org/10.3390/v11010051

Find Other Styles
Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Article Access Map by Country/Region

1
Back to TopTop