Abstract Eight thaumatin-like proteins of barley (Hordeum vulgare L.) (TLP1–TLP8) were detected in Drechslera teres infected leaves by two-dimensional electrophoresis followed by N-terminal microsequencing: four of them are acidic; four are basic proteins. Partial amino acid sequence data were used to generate polymerase chain reaction (PCR) clones employed for the isolation of four novel, nearly full-length cDNA sequences encoding TLP4, TLP6, TLP 7, and TLP 8. The cDNAs are characterized by sequence sites of very high GC content and they encode proteins with 171–233 amino acid residues. The N-termini of the deduced proteins were preceded by putative signal peptides of 22–25 amino acid residues. With a Clustal W based dendrogram similar sequences were assigned to those we obtained in this work.