Leptoglycin: A new Glycine/Leucine-rich antimicrobial peptide isolated from the skin secretion of the South American frog Leptodactylus pentadactylus (Leptodactylidae)

Sousa, Juliana Carvalho de; Berto, R.; Gois, Elicélia A.; Fontenele-Cardi, Nauíla C.; Honório-Júnior, José E.R.; Konno, Katsuhiro; Richardson, Michael; Rocha, Marcos F.G.; Camargo, Antônio A.C.M.; Pimenta, Daniel C.; Cardi, Bruno A.; Carvalho, Karine Maria Martins Bezerra

doi:10.1016/j.toxicon.2009.03.011

Cited by 59 publications

(54 citation statements)

References 55 publications

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“…The growth of the Grampositive bacterium S. aureus was slowed down in the presence of ctenidins to about 30% of the normal growth (data not shown), but was not completely inhibited. This selective activity against Gram-negative bacteria is in agreement with other glycine-rich AMPs [13,45]. The specificity for Gram-negative bacteria might be due to the composition of their outer membrane.…”

Section: Discussionsupporting

confidence: 84%

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: Discussionsupporting

confidence: 84%

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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“…More recently, glycine-leucine-rich peptides have been isolated from skin secretions of L. laticeps [68] and L. pentadactylus [69] that show limited structural similarity to the plasticins, previously identified only in phyllomedusid frogs of the family Hylidae. Like the plasticins, the peptide from L. laticeps adopts a random coil conformation in water, a b-sheet structure in methanol, and an alphahelical conformation in 50% trifluoroethanol-water.…”

Section: Leptodactylidaementioning

confidence: 99%

“…Like the plasticins, the peptide from L. laticeps adopts a random coil conformation in water, a b-sheet structure in methanol, and an alphahelical conformation in 50% trifluoroethanol-water. This component lacked antimicrobial activity [68], but the peptide from L. pentadactylus, unexpectedly in view of its low cationicity, was active against Gram-negative bacteria [69].…”

Section: Leptodactylidaementioning

confidence: 99%

Structural diversity and species distribution of host-defense peptides in frog skin secretions

Conlon

2011

Cell. Mol. Life Sci.

170

147

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Cationic peptides that adopt an amphipathic α-helical conformation in a membrane-mimetic environment are synthesized in the skins of many frog species. These peptides often display cytolytic activities against bacteria and fungi consistent with the idea that they play a role in the host's system of defense against pathogenic microorganisms, but their importance in the survival strategy of the animal is not clearly understood. Despite the common misconception that antimicrobial peptides are synthesized in the skins of all anurans, the species distribution is sporadic, suggesting that their production may confer some evolutionary advantage to the organism but is not necessary for survival. The low potency of many frog skin antimicrobial peptides is consistent with the hypothesis that cutaneous symbiotic bacteria may provide the major system of defense against pathogenic microorganisms in the environment with antimicrobial peptides assuming a supplementary role in some species.

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“…fallax, Krintler, 1986), and the dermal glands of several species are known to produce defensive skin secretions (Cei et al, 1967), including antimicrobial peptides and other protein toxins found in L. fallax (Rollins-Smith et al, 2005;King et al, 2005a), L. labyrinthicus (Libério et al, 2014), L. laticeps (Conlon et al, 2009), L. latrans (Nascimento et al, 2004(Nascimento et al, , 2007Leite et al, 2010), L. pentadactylus (Habermehl, 1981;Barlow, 1998;King et al, 2005b;Limaverde et al, 2009;Sousa et al, 2009), L. syphax (Dourado et al, 2007). Similarly, the foam nests of L. vastus possess a novel surfactant protein (Hissa et al, 2008(Hissa et al, , 2014.…”

Section: Introductionmentioning

confidence: 99%

Systematics of the Neotropical GenusLeptodactylusFitzinger, 1826 (Anura: Leptodactylidae): Phylogeny, the Relevance of Non-molecular Evidence, and Species Accounts

Sá

Grant

Camargo

et al. 2014

South American Journal of Herpetology

133

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Leptoglycin: A new Glycine/Leucine-rich antimicrobial peptide isolated from the skin secretion of the South American frog Leptodactylus pentadactylus (Leptodactylidae)

Cited by 59 publications

References 55 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

Structural diversity and species distribution of host-defense peptides in frog skin secretions

Systematics of the Neotropical GenusLeptodactylusFitzinger, 1826 (Anura: Leptodactylidae): Phylogeny, the Relevance of Non-molecular Evidence, and Species Accounts

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