Rondonin an antifungal peptide from spider (Acanthoscurria rondoniae) haemolymph

Riciluca, Katie Cristina Takeuti; Sayegh, Raphael Santa Rosa; Melo, Robson L.; Silva, P.I.

doi:10.1016/j.rinim.2012.03.001

Cited by 63 publications

(69 citation statements)

References 36 publications

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“…Antimicrobial peptides (AMPs) are a major part of the innate immune defense mechanism and have been extensively studied in the past 20 years. AMPs have broad-spectrum activity against different organisms including Gram-positive and Gram-negative bacteria (Zhu et al 2014; Dolashka et al 2011; Zhuang et al 2015), as well as fungi, viruses, parasites, and some cancer cells (Choi and Lee 2014; Bulmer et al 2010; Riciluca et al 2012; Badani et al 2014; Liu et al 2012; Adade et al 2013; Deng et al 2016). …”

Section: Introductionmentioning

confidence: 99%

Prediction and characterization of a novel hemocyanin-derived antimicrobial peptide from shrimp Litopenaeus vannamei

et al. 2018

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Hemocyanin, the multifunctional glycoprotein in the hemolymph of invertebrates, can generate various antimicrobial peptides (AMPs). Given the rising interest in the use of natural therapeutic agents such as AMPs, alternative and more efficient methods for their generation are being explored. In this work, free online software was first applied to predict the generation of antimicrobial peptides from the large subunit of Litopenaeus vannamei hemocyanin. Twenty potential antimicrobial peptides ranging from 1.5 to 1.9 kDa were predicted, five of which had α-helical structures and were selected for antibacterial activity testing. The results indicated that these five peptides had antibacterial activity against seven different bacteria. Of the five peptides, one peptide, designated L1, had the strongest antibacterial activity against both Gram-negative and Gram-positive bacteria. Moreover, CD and NMR data showed that L1 had both α-helical and β-turns structural composition, and that these structures were essential for L1’s antibacterial activity. Furthermore, SEM analysis revealed that peptide L1 had broad-spectrum activity against both Gram-positive and Gram-negative bacteria, as it could destroy the bacterial cell walls and kill the bacteria. Thus, L1 is a very potent antimicrobial peptide that can be exploited and used in antibacterial therapeutics.Electronic supplementary materialThe online version of this article (10.1007/s00726-018-2575-x) contains supplementary material, which is available to authorized users.

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Section: Introductionmentioning

confidence: 99%

Prediction and characterization of a novel hemocyanin-derived antimicrobial peptide from shrimp Litopenaeus vannamei

et al. 2018

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“…HeLp is the major constituent of Rhipicephalus ( Boophilus ) microplus hemolymph and has an important role in heme (obtained from blood feeding) binding and transport to other tissues [47] because the heme biosynthetic pathway is absent in these arachnids [48]. This sequence identity suggests that longipin might be generated from a precursor protein similarly to observed in the tarantula Acanthoscurria rondoniae [18] and Penaeus sp. shrimp [16], where cleavage of the hemocyanin C-terminal region originate peptides with antimicrobial activity.…”

Section: Discussionmentioning

confidence: 99%

“…They can be gene-encoded molecules, such as gomesin that is expressed as a pro-peptide [15], or originate from protein cleavage, such as has been observed in shrimp [16], ticks [17] and spiders [18]. These peptides can be grouped according to their physicochemical and structural characteristics [19] as well as their spectrum of activity.…”

Section: Introductionmentioning

confidence: 99%

Longipin: An Amyloid Antimicrobial Peptide from the Harvestman Acutisoma longipes (Arachnida: Opiliones) with Preferential Affinity for Anionic Vesicles

et al. 2016

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In contrast to vertebrate immune systems, invertebrates lack an adaptive response and rely solely on innate immunity in which antimicrobial peptides (AMPs) play an essential role. Most of them are membrane active molecules that are typically unstructured in solution and adopt secondary/tertiary structures upon binding to phospholipid bilayers. This work presents the first characterization of a constitutive AMP from the hemolymph of an Opiliones order animal: the harvestman Acutisoma longipes. This peptide was named longipin. It presents 18 aminoacid residues (SGYLPGKEYVYKYKGKVF) and a positive net charge at neutral pH. No similarity with other AMPs was observed. However, high sequence similarity with heme-lipoproteins from ticks suggested that longipin might be a protein fragment. The synthetic peptide showed enhanced antifungal activity against Candida guilliermondii and C. tropicalis yeasts (MIC: 3.8–7.5 μM) and did not interfered with VERO cells line viability at all concentrations tested (200–0.1 μM). This selectivity against microbial cells is related to the highest affinity of longipin for anionic charged vesicles (POPG:POPC) compared to zwitterionic ones (POPC), once microbial plasma membrane are generally more negatively charged compared to mammalian cells membrane. Dye leakage from carboxyfluorescein-loaded POPG:POPC vesicles suggested that longipin is a membrane active antimicrobial peptide and FT-IR spectroscopy showed that the peptide chain is mainly unstructured in solution or in the presence of POPC vesicles. However, upon binding to POPG:POPC vesicles, the FT-IR spectrum showed bands related to β-sheet and amyloid-like fibril conformations in agreement with thioflavin-T binding assays, indicating that longipin is an amyloid antimicrobial peptide.

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“…While Budnik et al reported a family of lycocitins from Lycosa singoriensis in 2004 [18], Kozlov et al discovered a family of latarcins from Lachesana tarabaevi in 2006 by chromatographic isolation as well as prediction from the spider venom expressed sequence tag data [19]. In 2012, both lycosin-I [20] and rondonin [21] were established as spider AMPs. Of note, antifungal rondonin, a 10-residue short peptide, is generated by cleaving a protein that delivers oxygen in the haemolymph of chelicerates.…”

Section: Discovery Of Spider and Scorpion Antimicrobial Peptidesmentioning

confidence: 99%

Insights into Antimicrobial Peptides from Spiders and Scorpions

Wang¹,

Wang

2016

PPL

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The venoms of spiders and scorpions contain a variety of chemical compounds. Antimicrobial peptides (AMPs) from these organisms were first discovered in the 1990s. As of May 2015, there were 42 spider’s and 63 scorpion’s AMPs in the Antimicrobial Peptide Database (http://aps.unmc.edu/AP). These peptides have demonstrated broad or narrow-spectrum activities against bacteria, fungi, viruses, and parasites. In addition, they can be toxic to cancer cells, insects and erythrocytes. To provide insight into such an activity spectrum, this article discusses the discovery, classification, structure and activity relationships, bioinformatics analysis, and potential applications of spider and scorpion AMPs. Our analysis reveals that, in the case of linear peptides, spiders use both glycine-rich and helical peptide models for defense, whereas scorpions use two distinct helical peptide models with different amino acid compositions to exert the observed antimicrobial activities and hemolytic toxicity. Our structural bioinformatics study improves the knowledge in the field and can be used to design more selective peptides to combat tumors, parasites, and viruses.

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Rondonin an antifungal peptide from spider (Acanthoscurria rondoniae) haemolymph

Cited by 63 publications

References 36 publications

Prediction and characterization of a novel hemocyanin-derived antimicrobial peptide from shrimp Litopenaeus vannamei

Prediction and characterization of a novel hemocyanin-derived antimicrobial peptide from shrimp Litopenaeus vannamei

Longipin: An Amyloid Antimicrobial Peptide from the Harvestman Acutisoma longipes (Arachnida: Opiliones) with Preferential Affinity for Anionic Vesicles

Insights into Antimicrobial Peptides from Spiders and Scorpions

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