Solution structure of a defense peptide from wheat with a 10-cysteine motif

Dubovskii, Peter V.; Vassilevski, Alexander A.; Slavokhotova, Anna A.; Одинцова, Т. И.; Grishin, Eugene V.; Egorov, Tsezi A.; Arseniev, Alexander S.

doi:10.1016/j.bbrc.2011.06.058

Cited by 41 publications

(49 citation statements)

References 34 publications

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“…Polycationic AMP are widely found not only in venoms, but also as part of the immune system in plants [51][52][53][54] and animals [55][56][57], where they often represent the first line of defense against invading microorganisms. Moreover, AMP are produced by bacteria as a tool for competition [58,59].…”

Section: Introductionmentioning

confidence: 99%

Latarcins: versatile spider venom peptides

Dubovskii

Vassilevski

Kozlov

et al. 2015

Cell. Mol. Life Sci.

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Arthropod venoms feature the presence of cytolytic peptides believed to act synergetically with neurotoxins to paralyze prey or deter aggressors. Many of them are linear, i.e., lack disulfide bonds. When isolated from the venom, or obtained by other means, these peptides exhibit common properties. They are cationic; being mostly disordered in aqueous solution, assume amphiphilic α-helical structure in contact with lipid membranes; and exhibit general cytotoxicity, including antifungal, antimicrobial, hemolytic, and anticancer activities. To suit the pharmacological needs, the activity spectrum of these peptides should be modified by rational engineering. As an example, we provide a detailed review on latarcins (Ltc), linear cytolytic peptides from Lachesana tarabaevi spider venom. Diverse experimental and computational techniques were used to investigate the spatial structure of Ltc in membrane-mimicking environments and their effects on model lipid bilayers. The antibacterial activity of Ltc was studied against a panel of Gram-negative and Gram-positive bacteria. In addition, the action of Ltc on erythrocytes and cancer cells was investigated in detail with confocal laser scanning microscopy. In the present review, we give a critical account of the progress in the research of Ltc. We explore the relationship between Ltc structure and their biological activity and derive molecular characteristics, which can be used for optimization of other linear peptides. Current applications of Ltc and prospective use of similar membrane-active peptides are outlined.

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Section: Introductionmentioning

confidence: 99%

Latarcins: versatile spider venom peptides

Dubovskii

Vassilevski

Kozlov

et al. 2015

Cell. Mol. Life Sci.

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“…Data concerning the three dimensional structure of peptide WAMP 1a obtained by the spectroscopic method of NMR also proves the similarity of the pep tide with the hevein like domain in chitinases of class 1 [51]. In general, all this points to the fact that the gene of the WAMP 1a peptide arose in evolution from the gene of ancient chitinase as a result of the deletion of a significant part of the catalytic domain.…”

Section: Defensinsmentioning

confidence: 84%

Defense peptides of plant immunity

Egorov

Одинцова

2012

Russ J Bioorg Chem

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Antimicrobial peptides (AMPs) are natural antibiotics produced by all living organisms to combat pathogens. They are important effector molecules of the immune system both in animals and plants. AMPs are diverse in structure and mode of action. Based on homology of amino acid sequences and 3D structures several AMP families have been distinguished. They are defensins, thionins, lipid transfer proteins, hevein- and knottin-like peptides, and cyclotides. AMPs display broad-spectrum antimicrobial activity and thus show promise for the development of disease- resistant crops by genetic engineering and for the production of new-generation drugs. In this paper, the properties of the main AMP families (defensins and hevein-like peptides) and of a new 4-Cys plant AMP family are reviewed.

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“…(Vogelsang and Barz 1993) -AGIAVYWGQN GNEGSLQDAC NTNNYQFVNIChitinase (Dolichos lablab) (Ye et al 2000) -GAVGSVINAS LFEQLLKHRN DQDPEGKGFY SYNAFITAChitinase-like protein (Panax notoginseng) (Lam and Ng 2001a, b; -EQFGKQAGMA LQPNG Chitinase-like protein (edible chive Allium tuberosum) (Lam et al 2000) -EQHGSQAGGA LHPGXLHYSK YGGYGGTTPD YYGDGQQ Chitinase-like protein (Acacia confusa seeds) (Lam and Ng 2010a) -EQHGRQAGGA LCMGG Chitin-binding protein (Ginkgo biloba) (Huang et al 2000) DPTCSVLGDKCNPGRCCSKINYCGACYQWRFGLTPAR Hevein-type chitin-binding protein (Triticum kiharae) (Dubovskii et al 2011) AQRCGDQARG AKCPNCLCCG KYGFCGSGDA YCGAGSCQSQ CRGC Hevein-type chitin-binding protein (Triticum kiharae) (Egorov et al 2005) AQRCGDQARG AKCPNCLCCG KYGFCGSGDA YCGAGSCQSQ CRGCR Introduction of a synthetic gene of the antimicrobial peptide thanatin into rice plants enabled the transformant to resist M. oryzae (Imamura et al 2010).…”

Section: Application In Ricementioning

confidence: 99%

Plant antifungal proteins and their applications in agriculture

Yan

Yuan

Jiang

et al. 2015

Appl Microbiol Biotechnol

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Fungi are far more complex organisms than viruses or bacteria and can develop numerous diseases in plants that cause loss of a substantial portion of the crop every year. Plants have developed various mechanisms to defend themselves against these fungi which include the production of low-molecular-weight secondary metabolites and proteins and peptides with antifungal activity. In this review, families of plant antifungal proteins (AFPs) including defensins, lectins, and several others will be summarized. Moreover, the application of AFPs in agriculture will also be analyzed.

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Solution structure of a defense peptide from wheat with a 10-cysteine motif

Cited by 41 publications

References 34 publications

Latarcins: versatile spider venom peptides

Latarcins: versatile spider venom peptides

Defense peptides of plant immunity

Plant antifungal proteins and their applications in agriculture

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