Antimicrobial Activity Spectrum, cDNA Cloning, and mRNA Expression of a Newly Isolated Member of the Cecropin Family from the Mosquito Vector Aedes aegypti

Lowenberger, Carl; Charlet, Maurice; Vizioli, Jacopo; Kamal, Sofie; Richman, Adam; Christensen, Bruce M.; Bulet, Philippe

doi:10.1074/jbc.274.29.20092

Cited by 110 publications

(122 citation statements)

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“…However, the absence of cysteines and the distribution of hydrophobic and polar amino acids in the primary structure indicate that the peptide may adopt a ␣-helical structure like that of insect cecropins. This prompts a comparison between the biological properties of spinigerin and two representatives of the amphipathic ␣Ϫhelical antimicrobial peptides: Aedes aegypti cecropin (8) and PGLa from Xenopus laevis (26) (see Table II). Spinigerin showed activity against two of the six Gram-positive bacteria tested, namely M. luteus and B. megaterium.…”

Section: Discussionmentioning

confidence: 99%

“…Cecropins, proline-rich, and glycine-rich peptides are essentially active against Gram-negative cells, but their activity spectrum sometimes includes Gram-positive bacteria as targets (6). Two recent reports have also indicated that cecropins can also exert antifungal properties (7,8). Among the open ended cysteine-rich peptides, insect defensins are the most widespread (9).…”

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confidence: 99%

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Insect Immunity

Lamberty¹,

Zachary²,

Lanot³

et al. 2001

Journal of Biological Chemistry

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210

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Two novel antimicrobial peptides, which we propose to name termicin and spinigerin, have been isolated from the fungus-growing termite Pseudacanthotermes spiniger (heterometabole insect, Isoptera). Termicin is a 36-amino acid residue antifungal peptide, with six cysteines arranged in a disulfide array similar to that of insect defensins. In contrast to most insect defensins, termicin is C-terminally amidated. Spinigerin consists of 25 amino acids and is devoid of cysteines. It is active against bacteria and fungi. Termicin and spinigerin show no obvious sequence similarities with other peptides. Termicin is constitutively present in hemocyte granules and in salivary glands. The presence of termicin and spinigerin in unchallenged termites contrasts with observations in evolutionary recent insects or insects undergoing complete metamorphosis, in which antimicrobial peptides are induced in the fat body and released into the hemolymph after septic injury.The termite species Pseudacanthotermes spiniger, like the other members of the Macrotermitinae, depends for its nutrition on a symbiotic fungus of the basidiomycete genus Termitomyces (1). This fungus grows inside the nests of the termites on piles of fecal pellets; it predigests the lignocellulosic substances and is responsible for food supply in cellulases. Macrotermitinae also live in symbiosis with anaerobic bacteria present in their posterior gut, which are in part responsible for the complete digestion of cellulose. In this environment inhabited with microorganisms, how do termites protect themselves?The first line of defense of insects against pathogens is the cuticle. Once this barrier has been breached, their defense reactions rely both on cellular and humoral mechanisms. The cellular aspects include phagocytosis and encapsulation of invading microorganisms (for a review, see Ref.2). The humoral facet involves the activation of proteolytic cascades leading to melanization and coagulation. In the evolutionary recent insect orders, the best characterized aspect of the humoral immune response is the rapid synthesis of antimicrobial peptides/ polypeptides by the fat body and certain blood cells and release of these factors into the hemolymph after bacterial challenge. Since the first report of an inducible antibacterial peptide from an insect, cecropin from the moth Hyalophora cecropia (3), more than 200 antimicrobial peptides/polypeptides have been characterized in insects. On the basis of their structural features, the peptides are classified into three classes: (i) linear peptides, devoid of cysteines and forming ␣-helices (the prototype of this family are the insect cecropins (4)), (ii) peptides with an overrepresentation in proline and/or glycine residues, and (iii) open-ended cyclic peptides containing cysteine residues (5). Cecropins, proline-rich, and glycine-rich peptides are essentially active against Gram-negative cells, but their activity spectrum sometimes includes Gram-positive bacteria as targets (6). Two recent reports have also indicated that c...

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Section: Discussionmentioning

confidence: 99%

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confidence: 99%

Insect Immunity

Lamberty¹,

Zachary²,

Lanot³

et al. 2001

Journal of Biological Chemistry

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210

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“…aegypti mosquitoes. The protein was active against a broad spectrum of Gram-negative bacteria but less so against Gram-positive bacteria and fungi (Lowenberger et al, 1999a). The Anopheles genome encodes four defensin genes (DEFs), four cecropins (CECs), one attacin and one gambicin (GAM1) .…”

Section: Pathogen Elimination Antimicrobial Peptides (Amps)mentioning

confidence: 99%

Innate immunity in the malaria vectorAnopheles gambiae:comparative and functional genomics

Osta

Christophides

Vlachou

et al. 2004

Journal of Experimental Biology

118

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“…These families include defensin and cecropin, which are the only classes of antimicrobial peptides so far reported in mosquitoes (10)(11)(12)(13)(14). Mosquitoes also contain genes encoding lysozyme (15)(16)(17).…”

Section: T He Mosquito Anopheles Gambiae Is the Major Vector Ofmentioning

confidence: 99%

Gambicin: A novel immune responsive antimicrobial peptide from the malaria vector Anopheles gambiae

Vizioli

Bulet

Hoffmann

et al. 2001

Proc. Natl. Acad. Sci. U.S.A.

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177

136

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A novel mosquito antimicrobial peptide, gambicin, and the corresponding gene were isolated in parallel through differential display-PCR, an expressed sequence tag (EST) project, and characterization of an antimicrobial activity in a mosquito cell line by reverse-phase chromatography. The 616-bp gambicin ORF encodes an 81-residue protein that is processed and secreted as a 61-aa mature peptide containing eight cysteines engaged in four disulfide bridges. Gambicin lacks sequence homology with other known proteins. Like other Anopheles gambiae antimicrobial peptide genes, gambicin is induced by natural or experimental infection in the midgut, fatbody, and hemocyte-like cell lines. Within the midgut, gambicin is predominantly expressed in the anterior part. Both local and systemic gambicin expression is induced during early and late stages of natural malaria infection. In vitro experiments showed that the 6.8-kDa mature peptide can kill both Gram-positive and Gram-negative bacteria, has a morphogenic effect on a filamentous fungus, and is marginally lethal to Plasmodium berghei ookinetes. An oxidized form of gambicin isolated from the cell line medium was more active against bacteria than the nonoxidized form from the same medium.Anopheles gambiae ͉ antimicrobial peptide ͉ innate immunity ͉ malaria

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Antimicrobial Activity Spectrum, cDNA Cloning, and mRNA Expression of a Newly Isolated Member of the Cecropin Family from the Mosquito Vector Aedes aegypti

Cited by 110 publications

References 43 publications

Insect Immunity

Insect Immunity

Innate immunity in the malaria vectorAnopheles gambiae:comparative and functional genomics

Gambicin: A novel immune responsive antimicrobial peptide from the malaria vector Anopheles gambiae

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