Antimicrobial activity of apitoxin, melittin and phospholipase A2 of honey bee (Apis mellifera) venom against oral pathogens

Leandro, Luís Fernando; Mendes, Carlos A.; Casemiro, Luciana Assirati; Vinholis, Adriana Helena Chicharo; Cunha, Wilson Roberto; Almeida, Rosana de; Martins, Carlos Henrique Gomes

doi:10.1590/0001-3765201520130511

Cited by 81 publications

(55 citation statements)

References 45 publications

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“…Recent studies prove that many venoms and venom components produced by different venomous animals show potential antibacterial activity. These include snake (Perumal Samy et al 2007;Al Ahmadi et al 2010;Ferreira et al 2011;Perumal Samy et al 2014b), spider (Haeberli et al 2000;Budnik et al 2004;Kozlov et al 2006;Benli and Yigit 2008), scorpion (Conde et al 2000;Torres-Larios et al 2002), honeybee (EL-Feel et al 2015;Leandro et al 2015) and wasp venoms (Jalaei et al 2014).…”

Section: The Antibiotic Potential Of Snake Venommentioning

confidence: 99%

Antibacterial properties of snake venom components

Bocian

Hus

2019

Chem. Pap.

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An increasing problem in the field of health protection is the emergence of drug-resistant and multi-drug-resistant bacterial strains. They cause a number of infections, including hospital infections, which currently available antibiotics are unable to fight. Therefore, many studies are devoted to the search for new therapeutic agents with bactericidal and bacteriostatic properties. One of the latest concepts is to search for this type of substances among toxins produced by venomous animals. In this approach, however, special attention is paid to snake venom because it contains molecules with antibacterial properties. Thorough investigations have shown that the phospholipases A 2 (PLA 2) and l-amino acids oxidases (LAAO), as well as fragments of these enzymes, are mainly responsible for the bactericidal properties of snake venoms. Some preliminary research studies also suggest that fragments of three-finger toxins (3FTx) are bactericidal. It has also been proven that some snakes produce antibacterial peptides (AMP) homologous to human defensins and cathelicidins. The presence of these proteins and peptides means that snake venoms continue to be an interesting material for researchers and can be perceived as a promising source of antibacterial agents.

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Section: The Antibiotic Potential Of Snake Venommentioning

confidence: 99%

Antibacterial properties of snake venom components

Bocian

Hus

2019

Chem. Pap.

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“…It is known that the antibacterial activity of commercial bee venom is 20 to 40 ug / ml (Leandro et al, 2015). However, it was presumed that some activities were changed during addition of excipient and drying process in the process of powdering bee venom.…”

Section: Results and Discussion:-mentioning

confidence: 99%

Study on Antibacterial Activity of Bee Venom.

Ha¹,

Noh²,

Bang³

et al. 2018

IJAR

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“…Antimicrobial peptides from poisonous animals are described for a number of scorpion peptides, as well as peptides from snakes, frogs, bees ( Apis sp. ), etc., as part of their host defense system [37,38,39,40,41,42,43,44,45,46]. For scorpions in particular, it has been proposed that the presence of antibacterial peptides protects the venom gland from pathogenic infections or potentiates toxin action [47].…”

Section: Discussionmentioning

confidence: 99%

Novel Conopeptides of Largely Unexplored Indo Pacific Conus sp.

et al. 2016

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Cone snails are predatory creatures using venom as a weapon for prey capture and defense. Since this venom is neurotoxic, the venom gland is considered as an enormous collection of pharmacologically interesting compounds having a broad spectrum of targets. As such, cone snail peptides represent an interesting treasure for drug development. Here, we report five novel peptides isolated from the venom of Conus longurionis, Conus asiaticus and Conus australis. Lo6/7a and Lo6/7b were retrieved from C. longurionis and have a cysteine framework VI/VII. Lo6/7b has an exceptional amino acid sequence because no similar conopeptide has been described to date (similarity percentage <50%). A third peptide, Asi3a from C. asiaticus, has a typical framework III Cys arrangement, classifying the peptide in the M-superfamily. Asi14a, another peptide of C. asiaticus, belongs to framework XIV peptides and has a unique amino acid sequence. Finally, AusB is a novel conopeptide from C. australis. The peptide has only one disulfide bond, but is structurally very different as compared to other disulfide-poor peptides. The peptides were screened on nAChRs, NaV and KV channels depending on their cysteine framework and proposed classification. No targets could be attributed to the peptides, pointing to novel functionalities. Moreover, in the quest of identifying novel pharmacological targets, the peptides were tested for antagonistic activity against a broad panel of Gram-negative and Gram-positive bacteria, as well as two yeast strains.

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Antimicrobial activity of apitoxin, melittin and phospholipase A2 of honey bee (Apis mellifera) venom against oral pathogens

Cited by 81 publications

References 45 publications

Antibacterial properties of snake venom components

Antibacterial properties of snake venom components

Study on Antibacterial Activity of Bee Venom.

Novel Conopeptides of Largely Unexplored Indo Pacific Conus sp.

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