Purification, characterization and gene expression of a glycine and proline‐rich antibacterial protein family from larvae of a beetle, <i>Allomyrina dichotoma</i>

Sagisaka, Aki; Miyanoshita, Akihiro; Ishibashi, Jun Ichiro; Yamakawa, Minoru

doi:10.1046/j.0962-1075.2001.00261.x

Cited by 61 publications

(47 citation statements)

References 35 publications

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“…The targets of glycine-rich peptides in bacteria and fungi are not clear, but can be diverse. Besides the classical membrane disruption or its depolarization [38], ctenidins could inhibit intracellular components as mentioned for proline-rich peptides [39] or could hamper bacterial cell division as suggested for the glycine-and proline-rich coleoptericins [40]. Another glycine-rich peptide family, the attacins, exerts its activity against Gram-negative bacteria by inhibiting the synthesis of an outer membrane protein by interfering with the transcription of its genes [41].…”

Section: Discussionmentioning

confidence: 99%

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: 99%

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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“…Both tenecin-4 and hemiptericin share ~22% identity to H. gloveri gloverin, but tenecin-4 has higher identity (22–24%) to H. virescens and T. ni gloverins than hemiptericin (15–17% identity). Other glycine-rich peptides are 7–10 kDa, such as P. terranovae and D. melanogaster diptericins (82 residues) (Dimarcq et al, 1988; Reichhart et al, 1989; Wicker et al, 1990), S. peregrina sarcotoxin-III (7 kDa) (Baba et al, 1987), Zophobas atratus and Allomyrina dichotoma coleoptericins (72–74 residues) (Bulet et al, 1991; Sagisaka et al, 2001), H. diomphalia holotricin-2 (72 residues) (Lee et al, 1994), Acalolepta luxuriosa acaloleptins (~8 kDa) (Imamura et al, 1999), and honeybee hymenoptaecin (93 residues) (Casteels et al, 1993). These glycine-rich peptides have activities against Gram-negative and Gram-positive bacteria.…”

Section: Gloverinsmentioning

confidence: 99%

Insect antimicrobial peptides and their applications

Huiuk

Chowdhury

Huang

et al. 2014

Appl Microbiol Biotechnol

482

459

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Insects are one of the major sources of antimicrobial peptides/proteins (AMPs). Since observation of antimicrobial activity in the hemolymph of pupae from the giant silk moths Samia Cynthia and Hyalophora cecropia in 1974 and purification of first insect AMP (cecropin) from H. cecropia pupae in 1980, over 150 insect AMPs have been purified or identified. Most insect AMPs are small and cationic, and they show activities against bacteria and/or fungi, as well as some parasites and viruses. Insect AMPs can be classified into four families based on their structures or unique sequences: the α-helical peptides (cecropin and moricin), cysteine-rich peptides (insect defensin and drosomycin), proline-rich peptides (apidaecin, drosocin and lebocin), and glycine-rich peptides/proteins (attacin and gloverin). Among insect AMPs, defensins, cecropins, proline-rich peptides and attacins are common, while gloverins and moricins have been identified only in Lepidoptera. Most active AMPs are small peptides of 20–50 residues, which are generated from larger inactive precursor proteins or pro-proteins, but gloverins (~14 kDa) and attacins (~20 kDa) are large antimicrobial proteins. In this mini-review, we will discuss current knowledge and recent progress in several classes of insect AMPs, including insect defensins, cecropins, attacins, lebocins and other proline-rich peptides, gloverins, and moricins, with a focus on structural-functional relationships and their potential applications.

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“…Coleoptericins display a bacteriostatic activity on a broad spectrum of bacteria, including both Gram-positive and Gram-negative bacteria [38][39][40]. In vitro incubation of Escherichia coli with weevil ColA impairs bacterial cell division and leads to cell gigantism [39,40].…”

Section: The Antimicrobial Peptide Coleoptericin a Keeps Endosymbiontmentioning

confidence: 99%

Antimicrobial peptides and cell processes tracking endosymbiont dynamics

Masson¹,

Zaidman-Rémy²,

Heddi³

2016

Phil. Trans. R. Soc. B

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One contribution of 13 to a theme issue 'Evolutionary ecology of arthropod antimicrobial peptides'. Many insects sustain long-term relationships with intracellular symbiotic bacteria that provide them with essential nutrients. Such endosymbiotic relationships likely emerged from ancestral infections of the host by free-living bacteria, the genomes of which experience drastic gene losses and rearrangements during the host-symbiont coevolution. While it is well documented that endosymbiont genome shrinkage results in the loss of bacterial virulence genes, whether and how the host immune system evolves towards the tolerance and control of bacterial partners remains elusive. Remarkably, many insects rely on a 'compartmentalization strategy' that consists in secluding endosymbionts within specialized host cells, the bacteriocytes, thus preventing direct symbiont contact with the host systemic immune system. In this review, we compile recent advances in the understanding of the bacteriocyte immune and cellular regulators involved in endosymbiont maintenance and control. We focus on the cereal weevils Sitophilus spp., in which bacteriocytes form bacteriome organs that strikingly evolve in structure and number according to insect development and physiological needs. We discuss how weevils track endosymbiont dynamics through at least two mechanisms: (i) a bacteriome local antimicrobial peptide synthesis that regulates endosymbiont cell cytokinesis and helps to maintain a homeostatic state within bacteriocytes and (ii) some cellular processes such as apoptosis and autophagy which adjust endosymbiont load to the host developmental requirements, hence ensuring a fine-tuned integration of symbiosis costs and benefits.This article is part of the themed issue 'Evolutionary ecology of arthropod antimicrobial peptides'.

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Purification, characterization and gene expression of a glycine and proline‐rich antibacterial protein family from larvae of a beetle, Allomyrina dichotoma

Cited by 61 publications

References 35 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

Insect antimicrobial peptides and their applications

Antimicrobial peptides and cell processes tracking endosymbiont dynamics

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