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Differential recruitment drives pathogen-mediated competition between species in an amphibian chytridiomycosis system.
Ecol Appl
January 2025
Centre for Planetary Health and Food Security, and School of Environment and Science, Griffith University, Southport, Queensland, Australia.
Pathogens that infect multiple host species have an increased capacity to cause extinctions through parasite-mediated apparent competition. Given unprecedented and continuing losses of biodiversity due to Batrachochytrium dendrobatidis (Bd), the causative fungus of the amphibian skin disease chytridiomycosis, a robust understanding of the mechanisms driving cross-species infection dynamics is essential. Here, we used stage-structured, susceptible-infected compartmental models to explore drivers of Bd-mediated apparent competition between two sympatric amphibians, the critically endangered Litoria spenceri and the non-threatened Litoria lesueurii.
View Article and Find Full Text PDFNovel Tryptophyllin Peptides from Physalaemus centralis Inhibit Oxidative Stress-Induced Endothelial Dysfunction in Rat Aorta Preparation.
Toxicon
January 2025
Applied Immunology and Morphology Research Centre, NuPMIA, Morphology Area, Faculty of Medicine, University of Brasília, UnB, Brasília, Distrito Federal, Brazil. Electronic address:
Amphibian skin is a rich source of molecules with biotechnological potential, including the tryptophyllin family of peptides. Here, we report the identification and characterization of two tryptophyllin peptides, FPPEWISR and FPWLLS-NH, from the skin of the Central Dwarf Frog, Physalaemus centralis. These peptides were identified through cDNA cloning and sequence comparison.
View Article and Find Full Text PDFA novel bombesin-related peptide modulates glucose tolerance and insulin secretion in non-obese and hypothalamic-obese rats.
Toxicon
January 2025
Universidade Estadual do Oeste do Paraná, Programa de Pós-Graduação em Biociências e Saúde (PPG-BCS), Cascavel, Brazil.
This study investigated the effects of a novel bombesin-related peptide (BR-b), derived from the skin of the Chaco tree frog (Boana raniceps), on glucose homeostasis in non-obese and hypothalamic-obese male rats. Hypothalamic obesity was induced in neonatal rats through high-dose administration of monosodium glutamate (MSG; 4 g/kg), while control animals (CTL) received an equimolar saline solution. At 70 days of age, both MSG and CTL groups underwent an oral glucose tolerance test (OGTT; 2 g/kg) with or without prior intraperitoneal administration of BR-b at doses of 0.
View Article and Find Full Text PDFCloning and Functional Analysis of Skin Host Defense Peptides from Yakushima Tago's Brown Frog () and Development of Serum Endotoxin Detection System.
Antibiotics (Basel)
November 2024
Department of Biology, Faculty of Science, Toho University, 2-2-1 Miyama, Funabashi-shi 274-8510, Chiba, Japan.
Amphibian skin is a valuable source of host defense peptides (HDPs). This study aimed to identify HDPs with novel amino acid sequences from the skin of and analyze their functions. cDNAs encoding HDP precursors were cloned and sequenced using RT-PCR and 3'-RACE.
View Article and Find Full Text PDFDesign, synthesis and activity evaluation of reduction-responsive anticancer peptide temporin-1CEa drug conjugates.
Bioorg Chem
January 2025
Key Laboratory of Structure-Based Drug Design & Discovery, Ministry of Education, School of Pharmaceutical Engineering, Shenyang Pharmaceutical University, Shenyang 110016, China. Electronic address:
Membranes that destroy anticancer peptides can bind to negatively charged cancer cell membranes through electrostatic interactions, destroying their functions and leading to cancer cell necrosis. Temporin-1CEa, obtained from the skin secretions of the Chinese frog Rana chensinensis, is an anticancer peptide with 17 amino acid residues that exhibits concentration-dependent cytotoxicity against a variety of cancer cell lines, although it has no obvious cytotoxicity to normal HUVECs. In this work, we designed and synthesized 12 derivative peptides through double-cysteine scanning of temporin-1CEa-truncated peptides.
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