AI Article Synopsis
Article Abstract
Prophylactic activity and side action of antiinfluenza lactoglobulin were studied under conditions of controlled epidemiological trial in 6361 persons during the epidemiological rise of influenza incidence. The data obtained pointed to the absence of any protective effect of antiinfluenza lactoglobulin. Marked allergenic properties of lactoglobulin and development of sensitization in the persons under observation were found during the study of the side-effect of the preparation. Thus, the absence of prophylactic efficacy and the sensitizing action of antiinfluenza lactoglobulin pointed to the inexpediency of its use for prophylactic and therapeutic purpose.
Download full-text PDF |
Source |
|---|
Publication Analysis
Top Keywords
Similar Publications
Chemically Modified Bovine β-Lactoglobulin as a Broad-Spectrum Influenza Virus Entry Inhibitor with the Potential to Combat Influenza Outbreaks.
Viruses
September 2022
Key Laboratory of Medical Molecular Virology of MOE/MOH, School of Basic Medical Sciences, Shanghai Public Health Clinical Center, Fudan University, 131 Dong An Rd., Xuhui District, Shanghai 200032, China.
Frequent outbreaks of the highly pathogenic influenza A virus (AIV) infection, together with the lack of broad-spectrum influenza vaccines, call for the development of broad-spectrum prophylactic agents. Previously, 3-hydroxyphthalic anhydride-modified bovine β-lactoglobulin (3HP-β-LG) was proven to be effective against human immunodeficiency virus (HIV) and severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) and it has also been used in the clinical control of cervical human papillomavirus (HPV) infections. Here, we show its efficacy in potently inhibiting infection by divergent influenza A and B viruses.
View Article and Find Full Text PDFBovine Lactoferrin Prevents Influenza A Virus Infection by Interfering with the Fusogenic Function of Viral Hemagglutinin.
Viruses
January 2019
National Centre for Innovative Technologies in Public Health, National Institute of Health, Viale Regina Elena 299, 00161 Rome, Italy.
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.
View Article and Find Full Text PDFLactoferrin-derived Peptides Active towards Influenza: Identification of Three Potent Tetrapeptide Inhibitors.
Sci Rep
September 2017
Department of Pharmacy, University of Salerno, Via Giovanni Paolo II 132, 84084, Fisciano, Italy.
Bovine lactoferrin is a biglobular multifunctional iron binding glycoprotein that plays an important role in innate immunity against infections. We have previously demonstrated that selected peptides from bovine lactoferrin C-lobe are able to prevent both Influenza virus hemagglutination and cell infection. To deeper investigate the ability of lactoferrin derived peptides to inhibit Influenza virus infection, in this study we identified new bovine lactoferrin C-lobe derived sequences and corresponding synthetic peptides were synthesized and assayed to check their ability to prevent viral hemagglutination and infection.
View Article and Find Full Text PDFBovine lactoferrin-derived peptides as novel broad-spectrum inhibitors of influenza virus.
Pathog Glob Health
March 2012
Department of Technology and Health, National Institute of Health, Rome, Italy.
Bovine lactoferrin (bLf) is a multifunctional glycoprotein that plays an important role in innate immunity against infections, including influenza. Here we have dissected bLf into its C- and N-lobes and show that inhibition of influenza virus hemagglutination and cell infection is entirely attributable to the C-lobe and that all major virus subtypes, including H1N1 and H3N2, are inhibited. By far-western blotting and sequencing studies, we demonstrate that bLf C-lobe strongly binds to the HA(2) region of viral hemagglutinin, precisely the highly conserved region containing the fusion peptide.
View Article and Find Full Text PDFBovine lactoferrin: involvement of metal saturation and carbohydrates in the inhibition of influenza virus infection.
Biochem Cell Biol
June 2012
Ultrastructural Infectious Pathology Section, Department of Technology and Health, National Institute of Health, Viale Regina Elena, 299, 00161 Rome, Italy.
Influenza is a highly contagious, acute respiratory illness, which represents one of the main plagues worldwide. Even though some antiviral drugs are available, the alarming increase of virus strains resistant to them highlights the need to find new antiviral compounds. As we have recently demonstrated that bovine lactoferrin (bLf) prevents influenza virus-induced apoptosis, in the present wor,k we have attempted to investigate in depth the mechanism of the anti-influenza virus effect of this protein.
View Article and Find Full Text PDFWant AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!