Vegetos

References

Aboye TL, Strömstedt AA, Gunasekera S, Bruhn JG, El-Seedi H, Rosengren KJ, Göransson U (2015) A cactus-derived toxin-like cystine knot peptide with selective antimicrobial activity. Eur J Chem Biol 16:1068–1077


Agrios GN (2005) Plant Pathology, 5th edn. Elsevier-Academic Press, Amsterdam


Allen A, Snyder AK, Preuss M, Nielsen EE, Shah DM, Smith TJ (2008) Plant defensins and virally encoded fungal toxin KP4 inhibit plant root growth. Planta 227:331–339


Alvarez CA, Barriga A, Albericio F, Romero MS, Guzmán F (2018) Identification of peptides in flowers of Sambucus nigra with antimicrobial activity against aquaculture pathogens. Molecules 23:1033


Asano T, Miwa A, Maeda K, Kimura M, Nishiuchi T (2013) The secreted antifungal protein thionin 2.4 in Arabidopsis thaliana suppresses the toxicity of a fungal fruit body lectin from Fusarium graminearum. PLoS Pathog 9:e10035


Badosa E, Ferre R, Francés J, Bardají E, Feliu L (2009) Sporicidal activity of synthetic antifungal undecapeptides and control of Penicillium rot of apples. Appl Environ Microbiol 75:5563–5569


Balls AK, Hale WS, Harris TH (1942) A crystalline protein obtained from a lipoprotein of wheat four. Ceram Chem 19:279–288


Bard GCV, Zottich U, Souza TAM, Ribeiro SFF, Dias GB, Pireda S, Da Cunha M, Rodrigues R, Pereira LS, Machado OLT, Carvalho AO, Gomes VM (2016) Purification, biochemical characterization, and antimicrobial activity of a new lipid transfer protein from Cofeacanephora seeds. Genet Mol Res. https://doi.org/10.4238/gmr15048859


Bechinger B (2004) Structure and Function of Membrane-Lytic Peptides. Critical Reviews in Plant Sci 23:271–292


Benko-Iseppon AM, Galdino SL, Calsa T Jr, Kido EA, Tossi A, Belarmino LC, Crovella S (2010) Overview on plant antimicrobial peptides. Curr Protein Pept Sci 11:181–188


Bogdanov IV, Finkina EI, Balandin SV, Melnikova DN, Stukacheva EA, Ovchinnikova TV (2015) Structural and functional characterization of recombinant isoforms of the lentil lipid transfer protein. Acta Naturae 7:65–73


Bogdanov IV, Shenkarev ZO, Finkina EI, Melnikova DN, Rumynskiy EI, Arseniev AS, Ovchinnikova TV (2016) A novel lipid transfer protein from the pea Pisum sativum: isolation, recombinant expression, solution structure, antifungal activity, lipid binding, and allergenic properties. BMC Plant Biol 16:10


Brogden KA (2005) Antimicrobial peptides: pore formers or metabolic inhibitors in bacteria? Nat Rev Microbiol 3:238–250


Campos ML, Li˜ao LM, Alves ESF, Migliolo L, Dias SC, Franco OL (2018) A structural perspective of plant antimicrobial peptides. Biochem J 475:3359–3375


Cavallarin L, Andreu D, San Segundo B (1998) Cecropin A-derived peptides are potent inhibitors of fungal plant pathogens. Mol Plant Microbe Interact 11:218–227


Chan YS, Wong JH, Fang EF, Pan WL, Ng TB (2012) An antifungal peptide from Phaseolus vulgaris cv. brown kidney bean. Acta Bioch Biophysica Sinica 44:307–315


Chandrashekhara NRS, Deepak S, Manjunath G, Shetty SH (2010) Thionins (PR protein 13) mediate pearl millet down mildew disease resistance. Arch Phytopathol Plant Protect 43:1356–1366


Cheng CS, Chouabe C, Eyraud V, Rahioui I, Royer C, Soulage C, Bonvallet R, Huss M, Gressent F (2011) New mode of action for a knottin protein bioinsecticide pea albumin 1 subunit b(PA1b) is the first peptidic inhibitor of V-ATP-ase. J Biol Chem 286:36291–36296


Craik DJ (2012) Host-Defense Activities of Cyclotides. Toxins 4:139–156


Cruz LP, Ribeiro SF, Carvalho AO, Vasconcelos IM, Rodrigue R, Da Cunha M (2010) Isolation and partial characterization of a novel lipid transfer protein (LTP) and antifungal activity of peptides from chilli pepper seeds. Protein Pept Lett 17:311–318


Daneshmand F, Zare-Zardini H, Ebrahimi L (2013) Investigation of the antimicrobial activities of Snakin-Z, a new cationic peptide derived from Zizyphus jujuba fruits. Nat Prod Res 27:2292–2296


De Beer A, Viver MA (2011) Four plant defensins from an indigenous South African Brassicaceae species display divergent activities against two test pathogens despite high sequence similarity in the encoding genes. BMC Res Notes 4:459–476


de Lucca AJ, Cleveland TE, Wedge DE (2005) Plant-derived antifungal proteins and peptides. Can J Microbiol 51:1001–1014


de Souza CE, Cardoso MHS, Sousa DA, Viana JC, Oliveira-Júnior NG, Miranda V, Franco OL (2014) The use of versatile plant antimicrobial peptides in agribusiness and human health. Peptides 55:65–78


Diz MS, Carvalho AO, Ribeiro SF, DaCunha M, Beltramini L, Rodrigues R (2011) Characterization, immune localization and antifungal activity of a lipid transfer protein from chili pepper (Capsicum annum) seeds with novel a-amylase inhibitory properties. Physiol Plantarum 142:233–246


Epple P, Apel K, Bohlmann H (1995) An Arabidopsis thaliana thionin gene is inducible via a signal transduction pathway different from that for pathogenesis-related proteins. Plant Physiol 109:813–820


Ferre R, Badosa E, Feliu L, Planas M, Montesinos E, Bardají E (2006) Inhibition of plant-pathogenic bacteria by short synthetic cecropin A-melittin hybrid peptides. Appl Environ Microbiol 72:3302–3308


García AN, Ayub ND, Fox AR, Gomez MC, Diéguez MJ, Pagano EM, Berini CA, Muschietti JP, Soto G (2014) Alfalfa snakin-1 prevents fungal colonization and probably coevolved with rhizobia. BMC Plant Biol 14:248


Gausing K (1987) Thionin genes specifcally expressed in barley leaves. Planta 171:241–246


Ghag SB, Shekhawat UKS, Ganapathi TR (2012) Petunia floral defensins with unique prodomains as novel candidates for development of Fusarium wilt resistance in transgenic banana plants. PLoS ONE 7:e39557


Haney EF, Straus SK, Hancock REW (2019) Reassessing the host defense peptide landscape. Front Chem 7:43


Hegedus N, Marx F (2013) Antifungal proteins: More than antimicrobials? Fungal Biol Rev 26:132–145


Herbel V, Sieber-Frank J, Wink M (2017) The antimicrobial peptide snakin-2 is upregulated in the defense response of tomatoes (Solanum lycopersicum) as part of the jasmonate-dependent signaling pathway. J Plant Physiol 208:1–6


Hintz T, Matthews KK, Di R (2015) The use of plant antimicrobial compounds for food preservation. BioMed Res Int 2015:246264


Hwang B, Hwang JS, Lee J, Lee DG (2010a) Antifungal properties and mode of action of psacotheasin, a novel knottin-type peptide derived from Psacothea hilaris. Biochem Biophys Res Commun 400:352–357


Hwang JS, Lee J, Hwang B, Nam SH, Yun EY, Kim SR, Lee DG (2010b) Isolation and characterization of psacotheasin, a novel knottin-type antimicrobial peptide, from Psacothea hilaris. J Microbiol Biotechnol 20:708–711


Islam B, Khan SN, Haque I, Alam M, Mushfiq M, Khan AU (2008) Novel anti-adherence activity of mulberry leaves: inhibition of Streptococcus mutans biofilm by 1-deoxynojirimycin isolated from Morus alba. J Antimicrob Chemother 62:751–757


Kerenga BK, McKenna JA, Harvey PJ, Quimbar P, Garcia-Ceron D, Lay FT, Phan TK, Veneer PK, Vasa S, Parisi K, Shafee TMA, van der Weerden NL, Hulett MD, Craik DJ, Anderson MA, Bleackley MR (2019) Salt-tolerant antifungal and antibacterial activities of the corn defensin ZmD32. Front Microbiol 10:795


Kini SG, Nguyen P, Weissbach S, Mallagaray A, Shin J, Yoon HS, Tam JP (2015) Studies on the chitin binding property of novel cysteine-rich peptides from Alternanthera sessilis. Biochem 54:6639–6649


Konarev AV, Anisimova IN, Gavrilova VA, Vachrusheva TE, Konechnaya GY, Lewis M, Shewry PR (2002) Serine proteinase inhibitors in the compositae: Distribution, polymorphism and properties. Phytochemistry 59:279–291


Le Nguyen D, Heitz A, Chiche L, Castro B, Boigegrain RA, Favel A, ColettiPreviero MA (1990) Molecular recognition between serine proteases and new bioactive microproteins with a knotted structure. Biochimie 72:431–435


Lohner K, Prossnigg F (2009) Biological activity and structural aspects of PGLa interaction with membrane mimetic systems. Biochem Biophys Acta 1788:1656–1666


Ma X, Iwanaka N, Masuda S, Karaike K, Egawa T, Hamada T, Toyoda T, Miyamoto L, Nakao K, Hayashi T (2009) Morus alba leaf extract stimulates 5-AMP-activated protein kinase in isolated rat skeletal muscle. J Ethnopharmacol 122:54–59


Malanovic N, Lohner K (2016) Antimicrobial Peptides Targeting Gram-Positive Bacteria Pharmaceuticals 9:59


Melnikova DN, Mineev KS, Finkina EI, Arseniev AS, Ovchinnikova TV (2016) A novel lipid transfer protein from the dill Anethum graveolens L.: Isolation, structure, heterologous expression, and functional characteristics. J Pept Sci 22:59–66


Moles AT, Peco B, Wallis IR, Foley WJ, Poore AGB, Seabloom EW, Vesk PA, Bisigato AJ, Cella-Pizarro L, Clark CJ, Cohen PS, Cornwell WK, Edwards W, Ejrnaes R, Gonzales-Ojeda T, Graae BJ, Hay G, Lumbwe FC, Maga˜na-Rodríguez B, Hui FKC, (2013) Correlations between physical and chemical defences in plants: Tradeoffs, syndromes, or just many different ways to skin a herbivorous cat? New Phytol 198:252–263


Montesinos E (2007) Antimicrobial peptides and plant disease control. FEMS Microbiol Lett 270:1–11


Nahirñak V, Almasia NI, Hopp HE, Vazquez-Rovere C (2012) Snakin/ GASA proteins involvement in hormone crosstalk and redox homeostasis. Plant Signal Behav 7:1004–1008


Nakatsuji T, Gallo RL (2011) Antimicrobial Peptides: Old Molecules with New Ideas. J Invest Dermatol 132(3 pt 2):887–895


Nawrot R, Barylski J, Nowicki G, Broniarczyk J, Buchwald W, Goździcka-Józefiak A (2014) Plant antimicrobial peptides. Folia Microbiol 59:181–196


Oomen RJ, Séveno-Carpentier E, Ricodeau N, Bournaud C, Conéjéro G, Paris N, Berthomieu P, Marquès L (2011) Plant defensin AhPDF1 is not secreted in leaves but it accumulates in intracellular compartments. New Phytol 192:140–150


Ovesen RG, Brandt KK, Göransson U, Nielsen J, Hansen HC, Cedergreen N (2011) Biomedicine in the environment: cyclotides constitute potent natural toxins in plants and soil bacteria. Environ Toxicol Chem 30:1190–2119


Pallaghy PK, Nielsen KJ, Craik DJ, Norton RS (1994) A common structural motif incorporating a cystine knot and a triple-stranded beta-sheet in toxic and inhibitory polypeptides. Protein Sci 3:1833–1839


Parsley NC, Kirkpatrick CL, Crittenden CM, Rad JG, Hoskin DW, Brodbelt JS, Hicks LM (2018) PepSAVI-MS reveals anticancer and antifungal cycloviolacins in Viola odorata. Phytochemistry 152:61–70


Pelegrini PB, Franco OL (2005) Plant gamma-thionins: novel insights on the mechanism of action of amulti-functional class of defense proteins. Int J Biochem Cell Biol 37:2239–2253


Pelegrini PB, Del Sarto RP, Silva ON, Franco OL, Grossi-De-Sa MF (2011) Antibacterial peptides from plants: what they are and how they probably work. Biochem Res Int 2011:250349


Pinheiro da Silva F, Machado MCC (2012) Antimicrobial peptides: Clinical relevance and therapeutic implications. Peptides 36:308–314


Pinto MEF, Najas JZG, Magalhães LG, Bobey AF, Mendonça JN, Lopes NP, Leme FM, Teixeira SP, Trovó M, Andricopulo AD, Koehbach J, Gruber CW, Cilli EM, Bolzani VS (2018) Inhibition of breast cancer cell migration by cyclotides isolated from Pombalia calceolaria. J Nat Prod 81:1203–1208


Portieles R, Ayra C, Gonzalez E, Gallo A, Rodriguez R, Chacón O, López Y, Rodriguez M, Castillo J, Pujol M, Enriquez G, Borroto C, Trujillo L, Thomma BP, Borrás-Hidalgo O (2010) NmDef02:a novel antimicrobial gene isolated from Nicotiana megalosiphon confers high level pathogen resistance under greenhouse and field conditions. Plant Biotechnol J 8:678–690


Pränting M, Lööv C, Burman R, Göransson U, Andersson DI (2010) The cyclotide cycloviolacin O2 from Viola odorata has potent bactericidal activity against gram-negative bacteria. J Antimicrob Chemother 65:1964–1971


Raheem N, Straus SK (2019) Mechanisms of Action for Antimicrobial Peptides with Antibacterial and Antibiofilm Functions. Front Microbiol 10:2866


Retzl B, Hellinger R, Muratspahić E, Pinto MEF, Bolzani VS, Gruber CW (2020) Discovery of a beetroot protease inhibitor to identify and classify plantderived cystine knot peptides. J Nat Prod 83:3305–3333


Rogozhin EA, Oshchepkova YI, Odintsova TI, Khadeeva NV, Veshkurova ON, Egorov TA, Grishin EV, Salikhov SI (2011) Novel antifungal defensins from Nigella sativa L. seeds. Plant Physiol Biochem 49:131–137


Rogozhin EA, Slezina MP, Slavokhotova AA, Istomina EA, Korostyleva TV, Smirnov AN, Grishin EV, Egorov TA, Odintsova TI (2015) A novel antifungal peptide from leaves of the weed Stellaria media L. Biochimie 116:125–132


Sagaram US, Pandurangi R, Kaur J, Smith TJ, Shah DM (2011) Structureactivity determinants in antifungal plant defensins msdef1 and MtDef4 with different modes of action against Fusarium graminearum. PLoS ONE. https://doi.org/10.1371/journal.pone.0018550


Schmidt M, Arendt EK, Thery TLC (2019) Isolation and characterisation of the antifungal activity of the cowpea defensin Cp-thionin II. Food Microbiol 82:504–514


Schmitt AJ, Sathoff AE, Holl C, Bauer B, Samac DA, Carter CJ (2018) The major nectar protein of Brassica rapa is a non-specific lipid transfer protein, BrLTP2.1, with strong antifungal activity. J Exp Bot 69:5587–5597


Schrader-Fisher G, Apel K (1994) Organ specific expression of highly divergent thionin variants that are distinct from the seed-specific crambin in the crucifer Crambe abyssinica. Mol Gen Genet 245:380–389


Selitrennikoff CP (2001) Antifungal proteins. Appl Environ Microbiol 67:2883–2894


Shwaiki LN, Arendt EK, Lynch KM (2020a) Anti-yeast activity and characterisation of synthetic radish peptides Rs-AFP1 and Rs-AFP2 against food spoilage yeast: Synthetic radish peptides against food spoilage yeast. Food Control 113: Article 107178.


Sinha M, Singh RP, Kushwaha GS, Iqbal N, Singh A, Kaushik S, Kaur P, Sharma S, Singh TP (2014) Current overview of allergens of plant pathogenesis related protein families. Sci World J 2014:543195


Souza AA, Costa AS, Campos DCO, Batista AHM, Sales GWP, Nogueira NAP, Alves KMM, Coelho-de-Souza AN, Oliveira HD (2018) Lipid transfer protein isolated from noni seeds displays antibacterial activity in vitro and improves survival in lethal sepsis induced by CLP in mice. Biochimie 149:9–17


Stec B (2006) Plant thionins—the structural perspective. Cell Mol Life Sci 63:1370–1385


Stec B, Markman O, Rao U, Hefron G, Henderson S, Vernon L, Brumfeld V, Teeter M (2004) Proposal for molecular mechanism of thionins deduced from physico-chemical studies of plant toxins. Chem Biol Drug Des 64:210–224


Stotz HU, Thomson J, Wang Y (2009) Plant defensins: defense, development and application. Plant Signal Behav 4:1010–1012


Tang L, Chen J, Zhou Z, Yu P, Yang Z, Zhong G (2015) Chlamydia secreted protease CPAF degrades host antimicrobial peptides. Microb Infect 17:402–408


Taveira GB, Mathias LS, da Motta OV, Machado OL, Rodrigues R, Carvalho AO, Teixeira-Ferreira A, Perales J, Vasconcelos IM, Gomes VM (2014) Thioninlike peptides from Capsicum annuum fruits with high activity against human pathogenic bacteria and yeasts. Biopolymers 102:30–39


Thevissen K, Warnecke DC, François IE, Leipelt M, Heinz E, Ott C, Zähringer U, Thomma BP, Ferket KK, Cammue BP (2004) Defensins from insects and plants interact with fungal glucosylceramides. J Biol Chem 279:3900–3905


Thevissen K, De Mello TP, Xu D, Blankenship J, Vandenbosch D, Idkowiak-Baladys J, Govaert G, Bink A, Rozental S, de Groot PW, Davis TR, Kumamoto CA, Vargas G, Nimrichter L, Coenye T, Mitchell A, Roemer T, Hannun YA, Cammue BP (2012) The plant defensin RsAFP2 induces cell wall stress, septin mislocalization and accumulation of ceramides in Candida albicans. Mol Microbiol 84:166–180


Thunberg E, Samuelsson G (1982) Isolation and properties of ligatoxin A, a toxic protein from the mistletoe Phoradendron liga. Acta Pharm Suec 19:285–292


Uhlig T, Kyprianou T, Martinelli FG, Oppici CA, Heiligers D, Hills D et al (2014) The emergence of peptides in the pharmaceutical business: from exploration to exploitation. EuPA Open Proteom 4:58–69


Utkina LL, Zhabon EO, Slavokhotova AA, Rogozhin EA, Shiian AN, Grishin EV, Pukhalskii VA (2010) Heterologous expression of a synthetic gene encoding a novel hevein type antimi crobial peptide of Leymus arenarius in Escherichia coli cells. Genetika 46:1645–1651


Utkina LL, Andreev YA, Rogozhin EA, Korostyleva TV, Slavokhotova AA, Oparin PB, Vassilevski AA, Grishin EV, Egorov TA, Odintsova TI (2013) Genes encoding 4-Cys antimicrobial peptides in wheat Triticum kiharae Dorof. et Migush.: multimodular structural organization instraspecifc variability distribution and role in defence. FEBS J 280:3594–3608


Vernon LP (1992) Pyrulariathionin physical properties, biological response and comparison to other thionins and cardiotoxin. J Toxicol 11:169–191


Wang C, Zhang Y, Zhang W, Yuan S, Ng T, Ye X (2019) Purifcation of an antifungal peptide from seeds of Brassica oleracea var. gongylodes and investigation of its antifungal activity and mechanism of action. Molecules 24:1337


Weiller F, Moore JP, Young P, Driouich A, Vivier MA (2016) The Brassicaceae species Heliophila coronopifolia produces root border-like cells that protect the root tip and secrete defensin peptides. Ann Bot 119:803–813


Wu WH, Di R, Matthews KR (2013) Activity of the plant-derived peptide IbAMP1 and the control of enteric foodborne pathogens. Food Control 33:142–147


Yeats TH, Rose JKC (2008) The biochemistry and biology of extracellular plant lipid-transfer proteins (LTPs). Protein Sci 17:191–198


Yount NY, Yeaman MR (2013) Peptide antimicrobials: cell wall as a bacterial target. Ann N Y Acad Sci 1277:127–138


Zarrabi M, Dalirfardouei R, Sepehrizade Z, Kermanshahi RK (2013) Comparison of the antimicrobial effects of semipurified cyclotides from Iranian Viola odorata against some of plant and human pathogenic bacteria. J Appl Microbiol 115:367–375


Zasloff M (2002) Antimicrobial peptides of multicellular organisms. Nature 415:389–395


Zhao M, Ma Y, Pan YH, Zhang CH, Yuan WX (2011) A hevein-like protein and a class I chitinase with antifungal activity from leaves of the paper mulberry. Biomed Chromatogr 25:908–912


Zottich U, Da Cunha M (2011) CarvalhoAéO, Dias GB, Silva Nádia CM, Santos IS, do Nacimento VV, Miguel Eílio C, Machado OLT, Gomes VM (2011) Purification, biochemical characterization and antifungal activity of a new lipid transfer protein (LTP) from Cofea canephora seeds with α-amylase inhibitor properties. Biochim Biophys Acta 1810(4):375–383