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Home / Equine Research Bank / J Biol Chem / Identification of Equine Lactadherin-derived Peptides That I...
The Journal of biological chemistry2015; 290(19); 12403-12414; doi: 10.1074/jbc.M114.620500

Identification of Equine Lactadherin-derived Peptides That Inhibit Rotavirus Infection via Integrin Receptor Competition.

Abstract: Human rotavirus is the leading cause of severe gastroenteritis in infants and children under the age of 5 years in both developed and developing countries. Human lactadherin, a milk fat globule membrane glycoprotein, inhibits human rotavirus infection in vitro, whereas bovine lactadherin is not active. Moreover, it protects breastfed infants against symptomatic rotavirus infections. To explore the potential antiviral activity of lactadherin sourced by equines, we undertook a proteomic analysis of milk fat globule membrane proteins from donkey milk and elucidated its amino acid sequence. Alignment of the human, bovine, and donkey lactadherin sequences revealed the presence of an Asp-Gly-Glu (DGE) α2β1 integrin-binding motif in the N-terminal domain of donkey sequence only. Because integrin α2β1 plays a critical role during early steps of rotavirus host cell adhesion, we tested a minilibrary of donkey lactadherin-derived peptides containing DGE sequence for anti-rotavirus activity. A 20-amino acid peptide containing both DGE and RGD motifs (named pDGE-RGD) showed the greatest activity, and its mechanism of antiviral action was characterized; pDGE-RGD binds to integrin α2β1 by means of the DGE motif and inhibits rotavirus attachment to the cell surface. These findings suggest the potential anti-rotavirus activity of equine lactadherin and support the feasibility of developing an anti-rotavirus peptide that acts by hindering virus-receptor binding.
© 2015 by The American Society for Biochemistry and Molecular Biology, Inc.
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Publication Date: 2015-03-26 PubMed ID: 25814665PubMed Central: PMC4424369DOI: 10.1074/jbc.M114.620500Google Scholar: Lookup
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Summary

This research summary has been generated with artificial intelligence and may contain errors and omissions. Refer to the original study to confirm details provided. Submit correction.

The research article discusses the discovery of a peptide derived from equine lactadherin that can inhibit rotavirus infection by competing with the virus for binding to integrin receptors.

Anti-Rotavirus Activity in Lactadherin

  • The research delves into the potential antiviral capabilities of lactadherin, a protein found in milk fat globule membranes, focusing on its source from donkeys.
  • Lactadherin has been observed to inhibit human rotavirus infection, a common cause of severe gastroenteritis in young children.
  • A significant component of the research involved the proteomic analysis of donkey milk proteins, with the intention to understand the amino acid sequence of donkey lactadherin.

Findings from Sequence Alignment

  • The researchers compared the sequence of lactadherin from humans, bovines, and donkeys and found the presence of a specific integrin-binding motif, Asp-Gly-Glu (DGE), in the N-terminal domain of donkey lactadherin.
  • The α2β1 integrin, to which the DGE motif binds, plays a critical role in the attachment of rotavirus to host cells.

Anti-Rotavirus Activity of Donkey Lactadherin-Derived Peptides

  • The study then investigated a library of peptides derived from donkey lactadherin that contained the DGE sequence. The goal was to evaluate their anti-rotavirus activity.
  • The peptide possessing the greatest activity was a 20-amino acid chain that contained both DGE and RGD motifs and was named pDGE-RGD.
  • The pDGE-RGD peptide demonstrated antiviral action through binding to the integrin α2β1 by means of the DGE motif, preventing the rotavirus from attaching to the cell surface.

Implications for Anti-Rotavirus Therapies

  • The study proposes the potential for equine lactadherin to inhibit rotavirus infections and paves the path for future development of an anti-rotavirus peptide-based treatment.
  • This therapy would work by hindering the binding of the virus to its receptors, thereby blocking its ability to infect host cells.

Cite This Article

APA
(2015). Identification of Equine Lactadherin-derived Peptides That Inhibit Rotavirus Infection via Integrin Receptor Competition. J Biol Chem, 290(19), 12403-12414. https://doi.org/10.1074/jbc.M114.620500

Publication

The Journal of biological chemistry
ISSN: 1083-351X
NlmUniqueID: 2985121R
Country: United States
Language: English
Volume: 290
Issue: 19
Pages: 12403-12414

Researcher Affiliations

MeSH Terms

  • Amino Acid Motifs
  • Amino Acid Sequence
  • Animals
  • Antigens, Surface / chemistry
  • Cattle
  • Cell Membrane / metabolism
  • Cell Survival
  • Equidae
  • Glycolipids / chemistry
  • Glycoproteins / chemistry
  • Horses
  • Humans
  • Inhibitory Concentration 50
  • Integrins / chemistry
  • Lipid Droplets
  • Membrane Glycoproteins / chemistry
  • Milk
  • Milk Proteins / chemistry
  • Molecular Sequence Data
  • Peptides / chemistry
  • Proteomics
  • Rotavirus / metabolism
  • Rotavirus Infections / drug therapy
  • Rotavirus Infections / metabolism
  • Sequence Homology, Amino Acid
  • Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization

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