Antifungal protein

Nielsen KK, Nielsen JE, Madrid S, Mikkelsen JD. New antifungal proteins from sugar beet Beta vulgaris L.) showing homology to non-specific lipid transfer proteins. Plant Mol Biol 1996 31 539-552. 

Asano, K., B. Svensson, and F. M. Polsen. Isolation and characterization of inhibitors of animal cell-free protein synthesis from barley seeds. Carlsberg Res Commun 1984 49(7) 619—626. Roberts, W. K., and C. P. Selitren-nikoff. Isolation and partial characterization of two antifungal proteins from barley. Biochim Biophys Acta 1986 880 161-170. 

Resorcinol, S-heptadecyl Seedling Resorcinol, 5 pentadecyl Seedling Resorcinol, 5-tridecyl Seedling Rhamnono l 4 lactone, L ppsois Rice antifungal protein 1 Seedling Sakuranetin Lf ° ° ° ... 

Waniska, R.D., Structure, phenolic compounds and antifungal proteins of Sorghum caryopses, in Proceedings of International Consultation, Chandrashekar, A., Bandyopadhyay, R., and Hall, A.J., Eds., ICRISTAT, India, 2000, 72. 

Salicylic acid is an inducer of antifungal proteins (Figure 4.38) and is proposed to activate the expression of SAR genes in the plant.21... 

Krebitz, M., B. Wagner, F. Ferreira, C. Peterbauer, N. Campillo, M. Witty, D. Kolarich, H. Steinkellner, O. Scheiner, and H. Breiteneder. 2003. Plant-based heterologous expression of Mai d 2, a thaumatin-like protein and allergen of apple (Malus domestica), and its characterization as an antifungal protein. J Mol Biol 329 (4) 721-730. 

Terras, F.R., Schoofs, H.M., De Bolle, M.F. et al. 1992. Analysis of two novel classes of plant antifungal proteins from radish (Raphanus sativus L.) seeds. J Biol Chem 267 15301-15309. 

Pennisetuin glaucum (pearl millet) (Poaceae) [seed] Pennisetum Cysteine PI (24 kDa 3 Cys antifungal protein) Papain [182]... 

A variety of other kinds of plant serine PIPs have been isolated [562-573] (Table 18), namely the arrowhead PIPs [562-566] and some representatives of some major classes of plant antifungal proteins, namely some defensins [121, 567, 568], some lipid transfer proteins (LTPs) [121, 169, 569, 570] and some napins [121, 571-573] (Table 18). The Sagittaria sagitdfolia (arrowhead) protease inhibitors A and B (API-A and API-B)... 

All prokaryote and eukaryote organisms are bounded by cell membranes that are basically phospholipid bilayers decorated with peripheral (loosely bound) and integral (tightly embedded) proteins. A variety of plant triterpenoid saponins (Table 12.3) and defensive antifungal proteins (Table 12.4) can directly interact with phospholipids and are accordingly likely to act by interfering with cell membrane structure, integrity and permeability. 

Napins and napin-like proteins are c. 14kDa, disulfide-rich, heterodimeric antifungal proteins that are structurally similar to the LTPs and which may function by interacting with membrane phospholipids. Indeed, the napins can be synergistic with plant defensive thionin proteins in damaging pathogenic fungi. Some napins have protease inhibitory activity as do some LTPs (Chapter 13). 

A novel antifungal protein, designated chrysancorin, was isolated from the seeds of Chrysanthemum coronarium var. spatiosum LH Bailey [259]. It inhibits the activity of human immunodeficiency virus-reverse transcriptase (HIV-RT). The protein also possesses antifungal activity towards Botrytis cinerea, Mycosphaerella arachidicola and Physalospora piricola, but not against Rhizoctonum solani, Fusarium oxysporum, Coprinus comatus and a variety of bacteria tested. 

Salzman, R.A., Tikhonova, I., Bordelon, B.P., Hasegawa, P.M. and Bressan, R.A. (1998) Coordinate accumulation of antifungal proteins and hexoses constitutes a developmental controlled defence response during fruit ripening in grape, Plant Physiol., 117, 465-472. 

Marx, E. Small, basic antifungal proteins secreted from filamentous ascomycetes a comparative study regarding expression, structure, function and potential application. Appl. Microbiol. Biotechnol. 2004, 65, 133-142... 

Theis, T, Marx, F., Salvenmoser, W, Stahl, U., Meyer, V. New insights into the target site and mode of action of the antifungal protein of Aspergillus giganteus. Res. Microbiol. 2005, 156, 47-56... 

Wang, X., Bunkers, G.J. Potent heterologous antifungal proteins from cheeseweed [Malva parviflora). Biochem. Biophys. Res. Commun. 2000, 279, 669-673... 

Landon, C., Pajon, A., Vovelle, F., Sodano, P. The active site of drosomycin, a small insect antifungal protein, delineated by comparison with the modeled structure of RS-AFP2, a plant antifungal protein. /. Pept. Res. 2000, 56, 231-238... 

Theis, T, Stahl, U. Antifungal proteins targets, mechanisms and prospective applications. Cell. Mol. Life Sci. 2004, 61, 437-455... 

Roberts, W.K. Laue, B.E. Selitrennikoff, C.P. "Antifungal Proteins from Plants", In Antifungal Drugs, St. Georgiev, Ed., New York Academy of Sciences New York, 1988, 141-151. 

Deoxyribonucleic acid (tobacco clone cpb20-52 antifungal protein CPB 20 messenger RNA-complementary plus 5 - and 3 -flanking region fragment) XXII-2 ... 

Dolichin, an antifungal protein (Mr 28 kDa) isolated from the seeds of the field bean Dolichos lablab. It shows structural resemblance to chitinases, which also exhibit antifungal activity. Dolichin shows antifungal activity against Rhizoctonia solani, Fusarium oxysporum, and Coprinus coma-tus. Furthermore, dolichin is able to inhibit HIV reverse transcriptase, and a- and fi-glucosidases associated with HIV infection... 

Canodermin, an antifungal protein (Mr 15 kDa) from fruiting bodies of the medicinal mushroom Ganoderma lucidum. Gan-odermin inhibited the mycelial growth of Botrytis cinera, Fusarium oxysporum, and Physalospora piricola [H. Wang, T. B. Ng, Peptides 2005, 27, 27]. 

X. A. Ye, R. H. Huang, X. Z. Liu, Y. Zhang, and D. C. Wang, Crystal structure of a novel antifungal protein distinct with five disulfide bridges from Eucommia ulmoides—Oliver at an atomic resolution, J. Struct. Biol., 148 (2004) 86-97. 

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