Apidaecins: antibacterial peptides from honeybees.

Casteels, Peter; Ampè, Christophe; Jacobs, Franciscus; Vaeck, Mark; Tempst, Paul

doi:10.1002/j.1460-2075.1989.tb08368.x

Cited by 428 publications

(323 citation statements)

References 17 publications

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“…The molecular weights of dominulins are similar to those of apidaecins, inducible hemolymph peptides with antibiotic activities reported for several Hy- menopterans [28]. However both the amino acid composition and sequence of apidaecins strongly differ from dominulins.…”

Section: Discussionsupporting

confidence: 67%

Dominulin A and B: Two new antibacterial peptides identified on the cuticle and in the venom of the social paper waspPolistes dominulususing MALDI-TOF, MALDI-TOF/TOF, and ESI-ion trap

Turillazzi

Mastrobuoni

Dani

et al. 2006

J. Am. Soc. Mass Spectrom.

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Two new antibacterial peptides, denominated as Dominulin A and B, have been found on the cuticle and in the venom of females of the social paper wasp Polistes dominulus. The amino acidic sequence of the two peptides, determined by mass spectrometry, is INWKKIAE VGGKIL SSL for Dominulin A (MW ϭ 1854 Da) and INWKKIAEIGKQVL SAL (MW ϭ 1909 Da) for Dominulin B. Their presence on the cuticle was confirmed using MALDI-TOF by means of micro-extractions and direct analyses on body parts. The presence in the venom and the primary structure of the dominulins suggest their classification in the mastoparans, a class of peptides found in the venom of other Aculeate hymenoptera. Their antimicrobial action against Gramϩ and GramϪ bacteria fits in the range of the best natural antimicrobial peptides. Dominulins can represent an important defense of the colony of Polistes dominulus against microbial pathogens. (J Am Soc Mass Spectrom 2006, 17, 376 -383)

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Section: Discussionsupporting

confidence: 67%

Dominulin A and B: Two new antibacterial peptides identified on the cuticle and in the venom of the social paper waspPolistes dominulususing MALDI-TOF, MALDI-TOF/TOF, and ESI-ion trap

Turillazzi

Mastrobuoni

Dani

et al. 2006

J. Am. Soc. Mass Spectrom.

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“…In contrast to penaeidin-1 and -2, penaeidin-3 is NH 2 -terminally blocked by a pyroglutamic acid. Identical NH 2 -terminal blocking amino acids have already been observed in other antimicrobial peptides such as hymenoptaecin (36) or some bovine ␤-defensins (43). The analysis of penaeidin-2 and -3 cDNAs showed the presence of a glycine codon at final position in the ORF.…”

Section: Table I Amino Acid Sequence Deduced From the Nanoes-ms-ms Stmentioning

confidence: 66%

“…The MIC values are expressed as intervals of concentration (a-b), where a is the highest concentration at which bacteria are growing and b is the lowest concentration that causes 100% of growth inhibition (36).…”

Section: Antimicrobial Assaysmentioning

confidence: 99%

“…For the time being and for convenience, these antimicrobial peptides are tentatively classified into four distinct groups based on amino acid sequences, secondary structures, and functional similarities: (i) linear basic peptides forming amphipathic ␣-helices including the cecropins, the first antimicrobial peptide isolated from insect hemolymph (for review see Ref. 9); (ii) peptides with one to six intramolecular disulfide bridges including the arthropod defensins (10), antifungal peptides from Drosophila, drosomycin (11) and metchnikowin (12), thanatin from Podisus (13), tachyplesin, big defensin and tachycitin from limulus (14 -16), and other cysteine-rich antimicrobial peptides isolated from a scorpion (17) and from a bivalve mollusk (18,19); (iii) prolinerich peptides, among them the apidaecins and abaecins from Hymenoptera (20,21) and drosocin from Drosophila hemolymph (22); (iv) glycine-rich antimicrobial peptides or polypeptides (9 -30 kDa) such as the attacins (23), diptericin (24) and sarcotoxins (25). The mode of action, the broad activity, the molecular diversity, and the noncytotoxicity of all these circulating antimicrobial peptides make them very attractive as therapeutic agents for pharmaceutical or agricultural applications (26,27).…”

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confidence: 99%

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Penaeidins, a New Family of Antimicrobial Peptides Isolated from the Shrimp Penaeus vannamei (Decapoda)

Destoumieux

Bulet

Loew

et al. 1997

Journal of Biological Chemistry

375

247

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We report here the isolation of three members of a new family of antimicrobial peptides from the hemolymph of shrimps Penaeus vannamei in which immune response has not been experimentally induced. The three molecules display antimicrobial activity against fungi and bacteria with a predominant activity against Gram-positive bacteria. The complete sequences of these peptides were determined by a combination of enzymatic cleavages, Edman degradation, mass spectrometry, and cDNA cloning using a hemocyte cDNA library. The mature molecules (50 and 62 residues) are characterized by an NH 2 -terminal domain rich in proline residues and a COOH-terminal domain containing three intramolecular disulfide bridges. One of these molecules is post-translationally modified by a pyroglutamic acid at the first position. Comparison of the data obtained from the cDNA clones and mass spectrometry showed that two of these peptides are probably COOHterminally amidated by elimination of a glycine residue. These molecules with no evident homology to other hitherto described antimicrobial peptides were named penaeidins.

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“…1) (33)(34)(35)(36)(37)(38). Their mode of action is unknown at present; in the case of apidaecin and of drosocin, which are proline-rich peptides isolated from honey-bees and from Drosophila, respectively, all-D isoforms are i n a~t i v e (~~,~O ) suggesting that the native peptides act via chiral receptors.…”

Section: (B) Drosomycinmentioning

confidence: 99%

Antimicrobial peptide defense in Drosophila

1997

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Drosophila responds to a septic injury by the rapid synthesis of antimicrobial peptides. These molecules are predominantly produced by the fat body, a functional equivalent of mammalian liver, and are secreted into the hemolymph where their concentrations can reach up to 100 μM. Six distinct antibacterial peptides (plus isoforms) and one antifungal peptide have been characterized in Drosophila and their genes cloned. The induction of the gene encoding the antifungal peptide relies on the spätzle/Toll/cactus gene cassette, which is involved in the control of dorsoventral patterning in the embryo, and shows interesting structural and functional similarities with cytokine‐induced activation of NF‐ϰB in mammalian cells. An additional pathway, dependent on the as yet unidentified imd (for immune‐deficiency) gene, is required for the full induction of the antibacterial peptide genes. Mutants deficient for the Toll and imd pathways exhibit a severely reduced survival to fungal and bacterial infections, respectively. Recent data on the molecular mechanisms underlying recognition of non‐self are also discussed in this review.

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Apidaecins: antibacterial peptides from honeybees.

Cited by 428 publications

References 17 publications

Dominulin A and B: Two new antibacterial peptides identified on the cuticle and in the venom of the social paper waspPolistes dominulususing MALDI-TOF, MALDI-TOF/TOF, and ESI-ion trap

Dominulin A and B: Two new antibacterial peptides identified on the cuticle and in the venom of the social paper waspPolistes dominulususing MALDI-TOF, MALDI-TOF/TOF, and ESI-ion trap

Penaeidins, a New Family of Antimicrobial Peptides Isolated from the Shrimp Penaeus vannamei (Decapoda)

Antimicrobial peptide defense in Drosophila

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