Purification, structure–function analysis, and molecular characterization of novel linear peptides from scorpion Opisthacanthus madagascariensis

Dai, Li; Corzo, Gerardo; Naoki, Hideo; Andriantsiferana, Marta; Nakajima, Terumi

doi:10.1016/s0006-291x(02)00423-0

Cited by 94 publications

(61 citation statements)

References 32 publications

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“…In a second step, the remaining glycine-extended peptide would be converted into a des-Gly peptide amine by a-amidation [28]. A similar amidation signal of X-Gly-Arg/Lys-Arg/Lys is also found in scorpion toxins [29,30]. Post-translational amidation of the C-terminus is a common modification of AMPs of chelicerates and crustaceans [13,14,19,31,32], making the peptides more stable and raising their positive net charge, an important feature of most AMPs.…”

Section: Discussionmentioning

confidence: 82%

Ctenidins: antimicrobial glycine-rich peptides from the hemocytes of the spider Cupiennius salei

Baumann

Kämpfer

Schürch

et al. 2010

Cell. Mol. Life Sci.

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Three novel glycine-rich peptides, named ctenidin 1-3, with activity against the Gram-negative bacterium E. coli, were isolated and characterized from hemocytes of the spider Cupiennius salei. Ctenidins have a high glycine content (>70%), similarly to other glycine-rich peptides, the acanthoscurrins, from another spider, Acanthoscurria gomesiana. A combination of mass spectrometry, Edman degradation, and cDNA cloning revealed the presence of three isoforms of ctenidin, at least two of them originating from simple, intronless genes. The full-length sequences of the ctenidins consist of a 19 amino acid residues signal peptide followed by the mature peptides of 109, 119, or 120 amino acid residues. The mature peptides are post-translationally modified by the cleavage of one or two C-terminal cationic amino acid residue(s) and amidation of the newly created mature C-terminus. Tissue expression analysis revealed that ctenidins are constitutively expressed in hemocytes and to a small extent also in the subesophageal nerve mass.

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Section: Discussionmentioning

confidence: 82%

Ctenidins: antimicrobial glycine-rich peptides from the hemocytes of the spider Cupiennius salei

Baumann

Kämpfer

Schürch

et al. 2010

Cell. Mol. Life Sci.

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“…Meanwhile, cytolytic peptides have been identified in the venoms of three out of four scorpion superfamilies. Purified and characterized cytolytic peptides have been described for Parabuthus schlechteri (Buthidae) [63,64], Pandinus imperator [59,65] and Opistophthalmus carinatus (Scorpionidae) [64], Opisthacanthus madagascariensis (Ischnuridae) [66] and Hadrurus aztecus (Iuridae) [67]. From the venom gland of the Chinese scorpion Buthus martensii (Buthidae) a full-length cDNA was isolated that encodes an insect defensin-like peptide named BmTXKS2 [68].…”

Section: Scorpionsmentioning

confidence: 99%

“…From the venom, two C-terminal truncated forms of both peptides, which lack the last two amino acid residues, were isolated. These nonamidated forms showed neither bactericidal nor hemolytic activity and were shown to be the result of proteolytic activity of the scorpion venom [66]. Analyses of the cDNA encoding the precursors of IsCT and IsTC2 revealed that, besides the signal peptide of 23 amino acid residues, both contained an unusual acidic propeptide (3 Glu/7 Asp) at the C-terminal with unknown function.…”

Section: Scorpionsmentioning

confidence: 99%

Antimicrobial and cytolytic peptides of venomous arthropods

Kuhn‐Nentwig

2003

Cellular and Molecular Life Sciences (CMLS)

187

131

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As a response to invading microorganisms, the innate immune system of arthropods has evolved a complex arrangement of constitutive and inducible antimicrobial peptides that immediately destroy a large variety of pathogens. At the same time, venomous arthropods have developed an additional offensive system in their venom glands to subdue their prey items. In this complex venom system, several enzymes, low-molecular-mass compounds, neurotoxins, antimicrobial and cytolytic peptides interact together, resulting in extremely rapid immobilization and/or killing of prey or aggressors. This review provides an overview of antimicrobial peptides identified in the hemolymph of venomous arthropods, and especially of cytolytic peptides in their venom. For these peptides a dual role is proposed: acting as antimicrobials as well as increasing the potency of the venom by influencing excitable cells.

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“…Chemical synthesis, characterization and CD spectra of the amino-terminal segments (residues 1 -9, named Janf1; residues 1 -35, named Jan-f3) of opiscorpine 1 were performed according to Dai et al [17].…”

Section: Chemical Synthesis and CD Spectramentioning

confidence: 99%

The scorpine family of defensins: gene structure, alternative polyadenylation and fold recognition

Zhu

Tytgat

2004

CMLS, Cell. Mol. Life Sci.

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Small cationic antimicrobial peptides (SCAMPs) as effectors of animal innate immunity provide the first defense against infectious pathogens. This class of molecules exists widely in invertebrate hemolymph and vertebrate skin secretion, but animal venoms are emerging as a new rich resource. Scorpine is a unique scorpion venom defensin peptide that has an extended amino-terminal sequence similar to cecropins. From the African scorpion Opistophthalmus carinatus venom gland, we isolated and identified several cDNAs encoding four new homologs of scorpine (named opiscorpines 1-4). Importantly, we show for the first time the existence of multiple opiscorpine mRNAs with variable 3' untranslated regions (UTRs) in the venom gland, which may be generated by alternative usage of polyadenylation signals. The complete opiscorpine gene structure including its promoter region is determined by genomic DNA amplification. Two large introns were found to be located within the 5' UTR and at the boundary of the mature peptide-coding region. Such a gene structure is distinct, when compared with other scorpion venom peptide genes. However, a comparative promoter analysis revealed that both opiscorpine and scorpion venom neurotoxins share a similar promoter organization. Sequence analysis and structural modeling allow us to group the scorpines and scorpion long-chain K-channel toxins together into one family that shares a similar fold with two distinct domains. The N-terminal cecropin-like domain displaying a clear antimicrobial activity implies that the scorpine family represents a group of real naturally occurring hybrids. Based on the phylogenetic analysis, a possible cooperative interaction between the N and C domains is elucidated, which provides an evolutionary basis for the design of a new class of anti-infectious drugs.

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Purification, structure–function analysis, and molecular characterization of novel linear peptides from scorpion Opisthacanthus madagascariensis

Cited by 94 publications

References 32 publications

Ctenidins: antimicrobial glycine-rich peptides from the hemocytes of the spider Cupiennius salei

Ctenidins: antimicrobial glycine-rich peptides from the hemocytes of the spider Cupiennius salei

Antimicrobial and cytolytic peptides of venomous arthropods

The scorpine family of defensins: gene structure, alternative polyadenylation and fold recognition

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