European Food Research and Technology

, Volume 242, Issue 4, pp 625–629 | Cite as

The MRJP1 honey glycoprotein does not contribute to the overall antibacterial activity of natural honey

Short Communication
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Abstract

A recent study has claimed that honey glycoproteins including major royal jelly protein 1 (MRJP1), the most abundant protein in honey, exhibit strong antibacterial activity at  μg/ml concentrations. These were shown to be effective against a broad spectrum of multidrug-resistant clinical isolates. In this study, we investigated the antibacterial activity of the protein content of three different sterile honey samples (manuka honey, Revamil source honey and honeydew honey) used in wound care, and characterised the antibacterial activity of purified MRJP1. Following ultrafiltration, honey samples contained different amounts of proteins. The most abundant protein was MRJP1. Honey proteins with a molecular weight (MW) above 10 kDa did not inhibit the growth of the laboratory strain Micrococcus luteus. Similarly, purified MRJP1 did not possess any antibacterial activity against M. luteus, Pseudomonas aeruginosa and Staphylococcus aureus in both an agar well diffusion assay and a broth microdilution assay. The results of this study indicate that honey proteins with a MW above 10 kDa, including MRJP1, do not possess direct antibacterial activity.

Keywords

Honey MRJP1 Wound Antibacterial efficacy 
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Notes

Acknowledgments

We thank Dr. Jaroslav Klaudiny (Institute of Chemistry, Slovak Academy of Sciences) for providing a polyclonal antibody against MRJP1. This study was supported by the Scientific Grant Agency of the Ministry of Education of the Slovak Republic and the Slovak Academy of Sciences VEGA 2/0007/14.

Compliance with ethical standards

Conflict of interest

None.

Compliance with Ethics Requirements

This article does not contain any studies with human or animal subjects.

References

  1. 1.
    Majtan J, Klaudiny J, Bohova J, Kohutova L, Dzurova M, Sediva M, Bartosova M, Majtan V (2012) Methylglyoxal-induced modifications of significant honeybee proteinous components in manuka honey: possible therapeutic implications. Fitoterapia 83:671–677CrossRefGoogle Scholar
  2. 2.
    Bucekova M, Valachova I, Kohutova L, Prochazka E, Klaudiny J, Majtan J (2014) Honeybee glucose oxidase—its expression in honeybee workers and comparative analyses of its content and H2O2-mediated antibacterial activity in natural honeys. Naturwissenschaften 101:661–670CrossRefGoogle Scholar
  3. 3.
    Di Girolamo F, D’Amato A, Righetti PG (2012) Assessment of the floral origin of honey via proteomic tools. J Proteom 75:3688–3693CrossRefGoogle Scholar
  4. 4.
    Bilikova K, Simuth J (2010) New criterion for evaluation of honey: quantification of royal jelly protein apalbumin 1 in honey by ELISA. J Agric Food Chem 58:8776–8781CrossRefGoogle Scholar
  5. 5.
    Schmitzova J, Klaudiny J, Albert S, Schroder W, Schrockengost W, Hanes J, Judova J, Simuth J (1998) A family of major royal jelly proteins of the honeybee Apis mellifera L. Cell Mol Life Sci 54:1020–1030CrossRefGoogle Scholar
  6. 6.
    Hojo M, Kagami T, Sasaki T, Nakamura J, Sasaki M (2010) Reduced expression of major royal jelly protein 1 gene in the mushroom bodies of worker honeybees with reduced learning ability. Apidologie 41:194–202CrossRefGoogle Scholar
  7. 7.
    Fontana R, Mendes MA, de Souza Monson B, Konno K, César LMM, Malaspina O (2004) Jelleines: a family of antimicrobial peptides from the royal jelly of honeybees (Apis mellifera). Peptides 25:919–928CrossRefGoogle Scholar
  8. 8.
    Kamakura M (2011) Royalactin induces queen differentiation in honeybees. Nature 473:478–483CrossRefGoogle Scholar
  9. 9.
    Kamakura M, Suenobu N, Fukushima M (2001) Fifty-seven-kDa protein in royal jelly enhances proliferation of primary cultured rat hepatocytes and increases albumin production in the absence of serum. Biochem Biophys Res Commun 282:865–874CrossRefGoogle Scholar
  10. 10.
    Matsui T, Yukiyoshi A, Doi S, Sugimoto H, Yamada H, Matsumoto K (2002) Gastrointestinal enzyme production of bioactive peptides from royal jelly protein and their antihypertensive ability in SHR. J Nutr Biochem 13:80–86CrossRefGoogle Scholar
  11. 11.
    Majtan J, Kovacova E, Bilikova K, Simuth J (2006) The immunostimulatory effect of the recombinant apalbumin 1-major honeybee royal jelly protein-on TNFα release. Int Immunopharmacol 6:269–278CrossRefGoogle Scholar
  12. 12.
    Brudzynski K, Sjaarda C, Lannigan R (2015) MRJP1-containing glycoproteins isolated from honey, a novel antibacterial drug candidate with broad spectrum activity against multi-drug resistant clinical isolates. Front Microbiol 16:711Google Scholar
  13. 13.
    Kwakman PH, te Velde AA, De Boer L, Speijer D, VandenbrouckeGrauls CM, Zaat SA (2010) How honey kills bacteria. FASEB J 24:2576–2582CrossRefGoogle Scholar
  14. 14.
    Majtan J, Kumar P, Majtan T, Walls AF, Klaudiny J (2010) Effect of honey and its major royal jelly protein 1 on cytokine and MMP-9 mRNA transcripts in human keratinocytes. Exp Dermatol 19:e73–e79CrossRefGoogle Scholar
  15. 15.
    Chua LS, Lee JY, Chan GF (2015) Characterization of the proteins in honey. Anal Lett 48:697–709CrossRefGoogle Scholar
  16. 16.
    Brudzynski K, Sjaarda C (2015) Honey glycoproteins containing antimicrobial peptides, Jelleins of the major royal jelly protein 1, are responsible for the cell wall lytic and bactericidal activities of honey. Plos One 10(4):e0120238CrossRefGoogle Scholar
  17. 17.
    Majtan J, Bohova J, Prochazka E, Klaudiny J (2014) Methylglyoxal may affect hydrogen peroxide accumulation in manuka honey through the inhibition of glucose oxidase. J Med Food 17:290–293CrossRefGoogle Scholar
  18. 18.
    Šimúth J (2001) Some properties of the main protein of honeybee (Apis meliffera) royal jelly. Apidologie 32:69–80CrossRefGoogle Scholar

Copyright information

© Springer-Verlag Berlin Heidelberg 2016

Authors and Affiliations

  1. 1.Institute of ZoologySlovak Academy of SciencesBratislavaSlovakia
  2. 2.Laboratory of Molecular Apidology and Apitherapy, Institute of Molecular BiologySlovak Academy of SciencesBratislavaSlovakia
  3. 3.Department of Microbiology, Faculty of MedicineSlovak Medical UniversityBratislavaSlovakia

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