Role of lysine residue at 7th position of wasp chemotactic peptides

doi:10.1016/0006-291X(90)92398-J

Biochemical and Biophysical Research Communications

Volume 168, Issue 2, 30 April 1990, Pages 844-849

https://doi.org/10.1016/0006-291X(90)92398-J Get rights and content

Abstract

Most of chemotactic peptides isolated from various kinds of wasp venom have lysine residue at 7th (or 8th) position, but only a chemotactic peptide from Icaria sp. has no basic amino acid residues in the sequence. The relation of chemotaxis with other biochemical activities such as superoxide generation and lysosomal enzyme release from guinea pig neutrophils was studied by the use of substitution analogs of Icaria chemotactic peptide at 7th position. Findings revealed two distinct ways of chemoattractant signal transduction in neutrophils.

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Cited by (11)

Protonectin (1-6): A novel chemotactic peptide from the venom of the social wasp Agelaia pallipes pallipes
2010, Toxicon
Citation Excerpt :
The mechanism involves a series of cellular events regulated by temporal and spatial presentation of attractant molecules to migrating leukocytes (Lee et al., 1999). Eukaryotic cells in general detect the presence of chemotactic stimuli through specific GPCRs located on the plasma membrane of the chemo-attracted cells, making the cell–peptide interaction a relatively specific process (Nagashima et al., 1990). Fig. 7 shows results for PMNL chemotaxis assays for Protonectin, Protonectin (1–6), for the standard peptide HR2 and for the mixture 1:1 Protonectin:Protonectin (1–6).
Peptides constitute the largest group of Hymenoptera venom toxins; some of them interact with GPCR, being involved with the activation of different types of leukocytes, smooth muscle contraction and neurotoxicity. Most of these toxins vary from dodecapeptides to tetradecapeptides, amidated at their C-teminal amino acid residue. The venoms of social wasps can also contains some tetra-, penta-, hexa- and hepta-peptides, but just a few of them have been structurally and functionally characterized up to now. Protonectin (ILGTILGLLKGL-NH₂) is a polyfunctional peptide, presenting mast cell degranulation, release of lactate dehydrogenase (LDH) from mast cells, antibiosis against Gram-positive and Gram-negative bacteria and chemotaxis for polymorphonucleated leukocytes (PMNL), while Protonectin (1–6) (ILGTIL-NH₂) only presents chemotaxis for PMNL. However, the mixture of Protonectin (1–6) with Protonectin in the molar ratio of 1:1 seems to potentiate the biological activities dependent of the membrane perturbation caused by Protonectin, as observed in the increasing of the activities of mast cell degranulation, LDH releasing from mast cells, and antibiosis. Despite both peptides are able to induce PMNL chemotaxis, the mixture of them presents a reduced activity in comparison to the individual peptides. Apparently, when mixed both peptides seems to form a supra-molecular structure, which interact with the receptors responsible for PMNL chemotaxis, disturbing their individual docking with these receptors. In addition to this, a comparison of the sequences of both peptides suggests that the sequence ILGTIL is conserved, suggesting that it must constitute a linear motif for the structural recognition by the specific receptor which induces leukocytes migration.
Characterization of two novel polyfunctional mastoparan peptides from the venom of the social wasp Polybia paulista
2009, Peptides
Hymenoptera venoms are complex mixtures of biochemically and pharmacologically active components such as biogenic amines, peptides and proteins. Polycationic peptides generally constitute the largest group of Hymenoptera venom toxins, and the mastoparans constitute the most abundant and important class of peptides in the venom of social wasps. These toxins are responsible for histamine release from mast cells, serotonin from platelets, and catecholamines and adenylic acids from adrenal chromafin cells. The present work reports the structural and functional characterization of two novel mastoparan peptides identified from the venom of the neotropical social wasp Polybia paulista. The mastoparans Polybia-MP-II and -III were purified, sequenced and synthesized on solid phase using Fmoc chemistry and the synthetic peptides used for structural and functional characterizations. Polybia-MP-II and -III are tetradecapeptides, amidated at their C-termini, and form amphipathic α-helical conformations under membrane-mimetic conditions. Both peptides were polyfunctional, causing pronounced cell lysis of rat mast cells and erythrocytes, in addition to having antimicrobial activity against both Gram-positive and Gram-negative bacteria.
Structural and functional characterization of two novel peptide toxins isolated from the venom of the social wasp Polybia paulista
2005, Peptides
Two novel inflammatory peptides were isolated from the venom of the social wasp Polybia paulista. They had their molecular masses determined by ESI-MS and their primary sequences were elucidated by Edman degradation chemistry as:
- •
  Polybia-MPI: I D W K K L L D A A K Q I L-NH₂ (1654.09 Da),
- •
  Polybia-CP: I L G T I L G L L K S L-NH₂ (1239.73 Da).
Both peptides were functionally characterized by using Wistar rat cells. Polybia-MPI is a mast cell lytic peptide, which causes no hemolysis to rat erythrocytes and presents chemotaxis for polymorphonucleated leukocytes (PMNL) and with potent antimicrobial action both against Gram-positive and Gram-negative bacteria. Polybia-CP was characterized as a chemotactic peptide for PMNL cells, presenting antimicrobial action against Gram-positive bacteria, but causing no hemolysis to rat erythrocytes and no mast cell degranulation activity at physiological concentrations.
Structural and functional characterization of N-terminally blocked peptides isolated from the venom of the social wasp Polybia paulista
2004, Peptides
Two novel peptides were isolated from the crude venom of the social wasp Polybia paulista, by using RP-HPLC under a gradient of MeCN from 5 to 60% (v/v) and named Polybine-I and -II. Further purification of these peptides under normal phase chromatography, rendered pure enough preparations to be sequenced by Edman degradation chemistry. However, both peptides did not interact with phenylisothiocyanate reagent, suggesting the existence of a chemically blocked N-terminus. Therefore, the sequences of both peptides were assigned by ESI-MS/MS under CID conditions, as follows: Polybine-I Ac-SADLVKKIWDNPAL-NH₂ (Mr 1610 Da) and Polybine-II Ac-SVDMVMKGLKIWPL-NH₂ (Mr 1657 Da). During the tandem mass spectrometry experiments, a loss of 43 a.m.u. was observed from the N-terminal residue of each peptide, suggesting the acetylation of the N-terminus. Subsequently, the peptides with and without acetylation were synthesized on solid phase and submitted to functional characterizations; the biological activities investigated were: hemolysis, chemotaxis of polymorphonucleated leukocytes (PMNL), mast cell degranulation and antibiosis. The results revealed that the acetylated peptides exhibited more pronounced chemotaxis of PMNL cells and mast cell degranulation than the respective non-acetylated congeners; no hemolytic and antibiotic activities were observed, irrespective to the blockage or not of the α-amino groups of the N-terminal residues of each peptide. Therefore, the N-terminal acetylation may be related to the increase of the inflammatory activity of both peptides.
Structural and biological characterization of two novel peptides from the venom of the neotropical social wasp Agelaia pallipes pallipes
2004, Toxicon
The venom of the neotropical social wasp Agelaia pallipes pallipes was fractionated by RP-HPLC resulting in the elution of seven fractions; the last two were re-fractionated under RP-HPLC by using isocratic elution conditions and the purity of the fractions were confirmed by using ESI-MS analysis. Both fractions are constituted of peptide components, which were sequenced by Edman degradation chemistry, resulting in the following sequences:
Protonectin I-L-G-T-I-L-G-L-L-K-G-L-NH₂
Agelaia-MP I-N-W-L-K-L-G-K-A-I-I-D-A-L-NH₂
Both peptides are manually synthesized on solid-phase and functionally characterized by using Wistar rats cells. Protonectin is a non-hemolytic chemotactic peptide for polymorphonucleated leukocytes (PMNL), presenting some mast cell degranulating activity and potent antimicrobial action both against Gram-positive and Gram-negative bacteria. Agelaia-MP was characterized as a hemolytic mast cell degranulator toxin, presenting a poor antimicrobial action and no chemotaxis for PMNL.
Arthropod venoms affecting cell signalling system
1993, Regulatory Peptides

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Role of lysine residue at 7th position of wasp chemotactic peptides

Abstract

J. Biol. Chem.

J. Biol. Chem.

J. Biol. Chem.

Soviet J. Bioorg. Chem.