Purification and characterization of antimicrobial and vasorelaxant peptides from skin extracts and skin secretions of the North American pig frog Rana grylio

Kim, Joseph B; Halverson, Thomas; Basir, Yousef J.; Dulka, Joseph G.; Knoop, Floyd C.; Abel, Peter W.; Conlon, J. Michael

doi:10.1016/s0167-0115(00)00107-5

Cited by 52 publications

(19 citation statements)

References 27 publications

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“…The peptide ALKAAPSPA showed 35% homology with the antimicrobial peptide Temporin-LT2 (Wang et al, 2009) which contains the same motif ALKA. The sequence of the peptide AILIIVMLFGR showed 40% homology with the following antifungal peptides: Temporin-SHa (Abbassi et al, 2008), Temporin 1Bya (Conlon et al, 2003) and Temporin-1Gc (Kim et al, 2000). The peptide AAAAVFLSLLAVGHCAAADFNATDADADFAGNGVDFNSSDAAV-YWGPWTKAR is encrypted in the cereal protein expansin-B4 (Q94LR4).…”

Section: Discussionmentioning

confidence: 99%

Antifungal activity of sourdough fermented wheat germ used as an ingredient for bread making

Rizzello¹,

Cassone²,

Coda³

et al. 2011

Food Chemistry

168

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Section: Discussionmentioning

confidence: 99%

Antifungal activity of sourdough fermented wheat germ used as an ingredient for bread making

Rizzello¹,

Cassone²,

Coda³

et al. 2011

Food Chemistry

168

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“…In support of this, temporins possess other interesting non-antimicrobial functions: (i) similar to the mammalian AMPs, b-defensins and cathelicidins [69,70], temporin A has chemotactic effects on human phagocytes, presumably mediated by cell surface receptor(s) [45]. This important link between the innate and adaptive immune system (by recruiting immune cells to the sites of infection) adds a beneficial characteristic to temporins as candidates for drug development; (ii) temporins from R. grylio induce relaxation of vascular tissue from the rat thoracic aorta [71]; (iii) temporins B and L modulate the hydrolytic activity of secretory phospholipase A 2 from bee venom and human lachrymal fluid, thus improving the efficacy of the immune response to infections [72]; (iv) temporin L binds purified lypopolysaccharide (LPS or endotoxin) in vitro and prevents lethality in rat models of septic shock [unpublished results]. Neutralization of LPS, released from Gram-negative bacteria during infection, may help to eliminate, during or after antimicrobial therapy, the risk of sepsis, a serious symptom which can easily result in mortality.…”

Section: Role Of Temporins In Host Defencementioning

confidence: 99%

Temporins, anti-infective peptides with expanding properties

Mangoni

2006

Cell. Mol. Life Sci.

149

127

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Antimicrobial peptides are effector molecules of the innate immune response of all pluricellular organisms, providing them with first-line defence against pathogens. Amphibian skin secretions represent one of the richest natural sources for such peptide antibiotics, and temporins, a large family of antimicrobial peptides from frog skin, are among the smallest ones found in nature to date. Their functional role and modes of action have been described, along with their interesting and unique properties. These properties make temporins good molecules for an in-depth understanding of host defence peptides in general. Furthermore, they are attractive templates for the future design of new therapeutics against infectious diseases with new modes of action, urgently needed due to the increasing resistance of microorganisms to the available drugs.

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“…Temporins are short (13-residue) peptides, with an amidated C terminus and with only one positively charged amino acid. They were first identified in R. temporaria skin secretions (31) and further detected in several North American Rana species, such as Rana clamitans (32), Rana luteiventris (33), Rana pipiens (33), and Rana grylio (34). Temporins, together with indolicidin, are among the smallest AMPs isolated so far from animal sources.…”

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confidence: 99%