Purification and characterization of Luffin P1, a ribosome-inactivating peptide from the seeds of Luffa cylindrica

Li, Feng; Yang, Xin-Xiu; Xia, Hengchuan; Zeng, Rong; Hu, Weiguo; Li, Zhen; Zhang, Zuchuan

doi:10.1016/s0196-9781(03)00173-6

Cited by 46 publications

(46 citation statements)

References 23 publications

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“…The peptides isolated by us from dill seeds had higher fungicidal activity than peptides from seeds of other plants [7,8]. The results confirm that dill seeds contain a powerful fungitoxic peptide that strongly inhibits the growth of pathogenic fungus in vitro with IC 50 1.3 µg/mL (peak 3 in Fig.…”

supporting

confidence: 60%

Isolation of biocidal peptides from Anethum graveolens seeds

Yili

Aisa²,

Imamu

et al. 2006

Chem Nat Compd

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supporting

confidence: 60%

Isolation of biocidal peptides from Anethum graveolens seeds

Yili

Aisa²,

Imamu

et al. 2006

Chem Nat Compd

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“…In the previous study, gel filtration chromatography results showed that this peptide formed homotetramer in hydrophobic buffer and depolymerized to homodimer in hydrophilic buffer. It was also proposed that the polymerization of Luffin P1 generated the folds required for its N-glycosidase activity (Li et al, 2003). Since the shape of Luffin P1 in solution is unknown, using gel filtration chromatography for mass analysis may be inaccurate.…”

Section: Biochemical Characterization Of Luffin P1mentioning

confidence: 99%

“…In addition to the aforementioned RIPs, small RIPs with a molecular weight of about or less than 10 kDa are by comparison much less well known and have been isolated only from bitter gourd seeds designated c-momorcharin (Pu et al, 1996), sponge gourd seeds designated Luffin P1 (Li et al, 2003), Luffin-S (Gao et al, 1994) and fresh brown pumpkin seeds designated a-moschin and b-moschin . No 3D structural information is available for these small RIPs, although amino acid analysis revealed that they have very unusual amino acid compositions and are characterized by a predominance of arginine and glutamate residues.…”

Section: Introductionmentioning

confidence: 99%

Structural characterization and anti-HIV-1 activities of arginine/glutamate-rich polypeptide Luffin P1 from the seeds of sponge gourd (Luffa cylindrica)

Yang

Sze

et al. 2011

Journal of Structural Biology

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Luffin P1, the smallest ribosome-inactivating peptide from the seeds of Luffa cylindrica was found to have anti-HIV-1 activity in HIV-1 infected C8166 T-cell lines and be able to bind with HIV Rev Response Element. Nuclear magnetic resonance spectroscopy revealed that the Luffin P1 comprises a helix-loop-helix motif, with the two alpha helices tightly associated by two disulfide bonds. Based on our findings, we conclude that unlike the well-studied ribosome-inactivating proteins, which exert their action through N-glycosidase activities, Luffin P1 demonstrates a novel inactivation mechanism probably through the charge complementation with viral or cellular proteins. Our work also provides a new scaffold for the design of novel inhibitors from a simple helical motif.

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“…The alfa-hairpin family includes peptides with diverse functions, such as antifungal activity (Nolde et al 2011;Slavokhotova et al 2014;Utkina et al 2013), inhibition of protein synthesis (Li et al 2003), or protease inhibition (Conners et al 2007;Oparin et al 2012). Although being variable in amino acid sequences, alfa-hairpinins share the same 4-cysteine motif CX(3)CX(1-15)CX(3)C. In lymegrass transcriptome we found 16 putative alfa-hairpinins with this specific motif.…”

Section: Alfa-hairpinsmentioning

confidence: 82%

Prediction of Leymus arenarius (L.) antimicrobial peptides based on de novo transcriptome assembly

2015

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Leymus arenarius is a unique wild growing Poaceae plant exhibiting extreme tolerance to environmental conditions. In this study we for the first time performed whole-transcriptome sequencing of lymegrass seedlings using Illumina platform followed by de novo transcriptome assembly and functional annotation. Our goal was to identify transcripts encoding antimicrobial peptides (AMPs), one of the key components of plant innate immunity. Using the custom software developed for this study that predicted AMPs and classified them into families, we revealed more than 160 putative AMPs in lymegrass seedlings. We classified them into 7 families based on their cysteine motifs and sequence similarity. The families included defensins, thionins, hevein-like peptides, snakins, cyclotide, alfa-hairpinins and LTPs. This is the first communication about the presence of almost all known AMP families in trascriptomic data of a single plant species. Additionally, cysteine-rich peptides that potentially represent novel families of AMPs were revealed. We have confirmed by RT-PCR validation the presence of 30 transcripts encoding selected AMPs in lymegrass seedlings. In summary, the presented method of pAMP prediction developed by us can be applied for relatively fast and simple screening of novel components of plant immunity system and is well suited for whole-transcriptome or genome analysis of uncharacterized plants.

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Purification and characterization of Luffin P1, a ribosome-inactivating peptide from the seeds of Luffa cylindrica

Cited by 46 publications

References 23 publications

Isolation of biocidal peptides from Anethum graveolens seeds

Isolation of biocidal peptides from Anethum graveolens seeds

Structural characterization and anti-HIV-1 activities of arginine/glutamate-rich polypeptide Luffin P1 from the seeds of sponge gourd (Luffa cylindrica)

Prediction of Leymus arenarius (L.) antimicrobial peptides based on de novo transcriptome assembly

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