Bee Venom: Overview of Main Compounds and Bioactivities for Therapeutic Interests

There is no author summary for this article yet. Authors can add summaries to their articles on ScienceOpen to make them more accessible to a non-specialist audience.

Abstract

Apitherapy is an alternate therapy that relies on the usage of honeybee products, most importantly bee venom for the treatment of many human diseases. The venom can be introduced into the human body by manual injection or by direct bee stings. Bee venom contains several active molecules such as peptides and enzymes that have advantageous potential in treating inflammation and central nervous system diseases, such as Parkinson’s disease, Alzheimer’s disease, and amyotrophic lateral sclerosis. Moreover, bee venom has shown promising benefits against different types of cancer as well as anti-viral activity, even against the challenging human immunodeficiency virus (HIV). Many studies described biological activities of bee venom components and launched preclinical trials to improve the potential use of apitoxin and its constituents as the next generation of drugs. The aim of this review is to summarize the main compounds of bee venom, their primary biological properties, mechanisms of action, and their therapeutic values in alternative therapy strategies.

Related collections

Most cited references 72

Record: found
Abstract: found
Article: not found

Wild bees enhance honey bees' pollination of hybrid sunflower.

Sarah Greenleaf, Claire Kremen (2006)

Pollinators are required for producing 15-30% of the human food supply, and farmers rely on managed honey bees throughout the world to provide these services. Yet honey bees are not always the most efficient pollinators of all crops and are declining in various parts of the world. Crop pollination shortages are becoming increasingly common. We found that behavioral interactions between wild and honey bees increase the pollination efficiency of honey bees on hybrid sunflower up to 5-fold, effectively doubling honey bee pollination services on the average field. These indirect contributions caused by interspecific interactions between wild and honey bees were more than five times more important than the contributions wild bees make to sunflower pollination directly. Both proximity to natural habitat and crop planting practices were significantly correlated with pollination services provided directly and indirectly by wild bees. Our results suggest that conserving wild habitat at the landscape scale and altering selected farm management techniques could increase hybrid sunflower production. These findings also demonstrate the economic importance of interspecific interactions for ecosystem services and suggest that protecting wild bee populations can help buffer the human food supply from honey bee shortages.

0 comments Cited 173 times – based on 0 reviews      Review now

Bookmark

Record: found
Abstract: found
Article: not found

Melittin: a membrane-active peptide with diverse functions.

Amitabha Chattopadhyay, H Raghuraman (2007)

Melittin is the principal toxic component in the venom of the European honey bee Apis mellifera and is a cationic, hemolytic peptide. It is a small linear peptide composed of 26 amino acid residues in which the amino-terminal region is predominantly hydrophobic whereas the carboxy-terminal region is hydrophilic due to the presence of a stretch of positively charged amino acids. This amphiphilic property of melittin has resulted in melittin being used as a suitable model peptide for monitoring lipid-protein interactions in membranes. In this review, the solution and membrane properties of melittin are highlighted, with an emphasis on melittin-membrane interaction using biophysical approaches. The recent applications of melittin in various cellular processes are discussed.

0 comments Cited 151 times – based on 0 reviews      Review now

Bookmark

Record: found
Abstract: found
Article: not found

Process of inducing pores in membranes by melittin.

Chin-Chang Hung, Jian-Tao Lee, Tom Huang … (2013)

Melittin is a prototype of the ubiquitous antimicrobial peptides that induce pores in membranes. It is commonly used as a molecular device for membrane permeabilization. Even at concentrations in the nanomolar range, melittin can induce transient pores that allow transmembrane conduction of atomic ions but not leakage of glucose or larger molecules. At micromolar concentrations, melittin induces stable pores allowing transmembrane leakage of molecules up to tens of kilodaltons, corresponding to its antimicrobial activities. Despite extensive studies, aspects of the molecular mechanism for pore formation remain unclear. To clarify the mechanism, one must know the states of the melittin-bound membrane before and after the process. By correlating experiments using giant unilamellar vesicles with those of peptide-lipid multilayers, we found that melittin bound on the vesicle translocated and redistributed to both sides of the membrane before the formation of stable pores. Furthermore, stable pores are formed only above a critical peptide-to-lipid ratio. The initial states for transient and stable pores are different, which implies different mechanisms at low and high peptide concentrations. To determine the lipidic structure of the pore, the pores in peptide-lipid multilayers were induced to form a lattice and examined by anomalous X-ray diffraction. The electron density distribution of lipid labels shows that the pore is formed by merging of two interfaces through a hole. The molecular property of melittin is such that it adsorbs strongly to the bilayer interface. Pore formation can be viewed as the bilayer adopting a lipid configuration to accommodate its excessive interfacial area.

0 comments Cited 106 times – based on 0 reviews      Review now

Bookmark

All references

Author and article information

Journal

Journal ID (nlm-ta): Molecules

Journal ID (iso-abbrev): Molecules

Journal ID (publisher-id): molecules

Title: Molecules

Publisher: MDPI

ISSN (Electronic): 1420-3049

Publication date (Electronic): 19 August 2019

Publication date Collection: August 2019

Volume: 24

Issue: 16

Electronic Location Identifier: 2997

Affiliations

[1 ]Laboratory of Applied Biotechnology (LBA3B), Azm Center for Research in Biotechnology and its Applications, EDST, Lebanese University, Tripoli 1300, Lebanon

[2 ]Mitochondrial and Cardiovascular Pathophysiology—MITOVASC, Team 2, Cardiovascular Mechanotransduction, UMR CNRS 6015, INSERM U1083, Angers University, 49045 Angers, France

[3 ]Department of Neuroscience, Institut de Biologie Paris Seine (IBPS), INSERM, CNRS, Sorbonne Université, F-75005 Paris, France

[4 ]Institut de Génétique et de Biologie Moléculaire et Cellulaire (IGBMC), INSERM U964, CNRS U7104, Université de Strasbourg, 67400 Illkirch, France

[5 ]Faculty of Agriculture & Veterinary Sciences, Lebanese University, Dekwaneh, Beirut 2832, Lebanon

[6 ]Institute of NeuroPhysiopathology, UMR 7051, Faculté de Médecine Secteur Nord, 51, Boulevard Pierre Dramard-CS80011, 13344-Marseille Cedex 15, France

[7 ]Faculty of Sciences 3, Michel Slayman Tripoli Campus, Lebanese University, Ras Maska 1352, Lebanon

Author notes

[* ]Correspondence: ziad.fajloun@ 123456ul.edu.lb ; Tel.: +961-6-21-3255

[†]

These authors contributed equally to this work.

Author information

Rim Wehbe https://orcid.org/0000-0003-0887-2279

Jean-Marc Sabatier https://orcid.org/0000-0002-9040-5647

Article

Publisher ID: molecules-24-02997

DOI: 10.3390/molecules24162997

PMC ID: 6720840

PubMed ID: 31430861

SO-VID: 5a3c9763-8ab3-432b-a09e-44f836164f5f

License:

Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license ( http://creativecommons.org/licenses/by/4.0/).

Bee Venom: Overview of Main Compounds and Bioactivities for Therapeutic Interests

Read this article at

Abstract

Related collections

Cancer Immunotherapy

Most cited references 72

Wild bees enhance honey bees' pollination of hybrid sunflower.

Melittin: a membrane-active peptide with diverse functions.

Process of inducing pores in membranes by melittin.

Author and article information

Journal

Affiliations

Author notes

Author information

Article

History

Categories

Comments

Comment on this article

Similar content 245

Cited by 73

Most referenced authors 996