Two antifungal thaumatin-like proteins from barley grain.
Antifungal activity has been associated with 2 immunochemically distinct proteins, protein R and S (Mr approximately 23 kDa; pI 9-10), which were isolated in pure form from barley grain. The proteins are homologous with thaumatin- and pathogenesis-related proteins of the PR5 family. The proteins inhibit growth of i.a. Trichoderma viride and Candida albicans in microtiter plate assays and act synergistically with barley grain chitinase C. Like maize zeamatin, protein R and S but not chitinase C retarded fungal growth in synergism with nikkomycin Z, a nucleoside-peptide inhibitor of fungal chitin synthesis. Although no inhibition of alpha-amylases or serine proteases could be associated with protein R or S the results indicate that the homologous maize grain bifunctional inhibitor of insect alpha-amylase and trypsin is very similar to or identical with maize zeamatin, which was proposed to have permeabilizing activity towards fungal membranes. Thus, in addition to the intensely sweet properties of thaumatin, multiple unrelated defense functions against insect and fungal pests can now be associated with the family of thaumatin-homologous proteins.
Department of Biochemistry and Nutrition, Technical University of Denmark, Lyngby.
J
J
Hejgaard
S
S
Jacobsen
I
I
Svendsen
D000595:Amino Acid Sequence; D000935:Antifungal Agents / Q000737:chemistry / Q000302:isolation & purification* / Q000494:pharmacology; D001467:Hordeum / Q000737:chemistry*; D007120:Immunochemistry; D005779:Immunodiffusion; D008969:Molecular Sequence Data; D010940:Plant Proteins / Q000737:chemistry / Q000302:isolation & purification* / Q000494:pharmacology; D016415:Sequence Alignment
D000935:Antifungal Agents; D010940:Plant Proteins