• Background and Aims Colleters are secretory structures consisting of a parenchymatic middle axis surrounded by a layer of palisade-like epidermal cells. Colleters occur in a large number of rubiaceous species. Their function is to protect the developing shoot apex. They are also taxonomically useful in the Rubiaceae. This study characterized the structure of the colleters of Simira glaziovii, S. pikia and S. rubra and the biochemistry of secretions in S. glaziovii. • Methods Stipules of the shoot apices of the three species studied were collected at Barragem de Saracuruna, in Rio de Janeiro state, Brazil. The samples were fixed according to the usual methods for light and electron microscopy. Secretion stipules of S. glaziovii were washed with 0·1 m Tris–HCl plus 0·1 %Triton X-100 to extract proteins and carbohydrates. • Key Results Colleters in these species are located at the base of the stipule. Each species shows a different pattern of distribution. They form as emergentia from the stipules. Simira glaziovii was different from the other two species because it exhibited vascular traces. The epidermal cells of colleters have dense cytoplasm, nuclei, small vacuoles, endoplasmic reticulum, Golgi apparatus, mitochondria and extraplasmic spaces if they are secretory. The outer cell wall of the mature colleters differs from the outer cell wall of stipule cells and immature colleters. Both carbohydrates and proteins were found in secretions from the stipules of S. glaziovii. • Conclusions Few ultrastructural differences were noted among the three species. These secretory structures not only protect the shoot apex, but also have taxonomic importance below the genus level.

Thionins are a family of plant antimicrobial peptides (AMPs), which participate in plant defense system against pathogens. Here we describe some aspects of the CaThi thionin-like action mechanism, previously isolated from Capsicum annuum fruits. Thionin-like peptide was submitted to antimicrobial activity assays against Candida species for IC50 determination and synergism with fluconazole evaluation. Viability and plasma membrane permeabilization assays, induction of intracellular ROS production analysis and CaThi localization in yeast cells were also investigated. CaThi had strong antimicrobial activity against six tested pathogenic Candida species, with IC50 ranging from 10 to 40 μg.mL−1. CaThi antimicrobial activity on Candida species was candidacidal. Moreover, CaThi caused plasma membrane permeabilization in all yeasts tested and induces oxidative stresses only in Candida tropicalis. CaThi was intracellularly localized in C. albicans and C. tropicalis, however localized in nuclei in C. tropicalis, suggesting a possible nuclear target. CaThi performed synergistically with fluconazole inhibiting all tested yeasts, reaching 100 % inhibition in C. parapsilosis. The inhibiting concentrations for the synergic pair ranged from 1.3 to 4.0 times below CaThi IC50 and from zero to 2.0 times below fluconazole IC50. The results reported herein may ultimately contribute to future efforts aiming to employ this plant-derived AMP as a new therapeutic substance against yeasts.