A review on the structure and function of plant thaumatin-like proteins

Abstract

Thaumatin-like proteins (TLPs), a subclass of pathogenesis-related proteins (PR5) distinguished by the unique and stable “TLP-fold” structure, are ubiquitously found across plants, animals, and fungi. TLPs play a pivotal role as effector molecules in plant antimicrobial defense, while their structural flexibility and involvement in complex regulatory networks allow them to integrate multiple phytohormone signals, including salicylic acid, jasmonic acid, ethylene, and abscisic acid. This enables a coordinated response to both biotic and abiotic stresses, positioning TLPs as an “integrative hub” in plant stress adaptation. This review synthesizes the current literature on gene functional validation, providing a systematic overview of the structural characteristics, evolutionary features, and regulatory mechanisms of the TLP family. It emphasizes the multifunctionality and molecular mechanisms of TLPs in disease resistance, stress tolerance, growth regulation, and their role as allergens. Additionally, it discusses the central role of TLPs in integrating stress responses and their potential applications in crop resistance breeding, offering valuable insights for future research.