Calcium and integrin-binding protein 1-like interacting with an integrin α-cytoplasmic domain facilitates cellular immunity in Helicoverpa armigera

Integrins are transmembrane receptor heterodimers composed of alpha and beta subunits. They are known to mediate extracellular signals to promote cell adhesion and spreading, and are therefore essential for cellular immunity. However, proteins that bind to integrin cytoplasmic domains and mediate intracellular signaling to promote cell adhesion require identification. Calcium and integrin-binding protein 1 (CIB1) that binds to the integrin alpha-cytoplasmic domain has rarely been examined in insects. In this study, we found that 20-hydroxyecdysone promoted cell phagocytosis and spreading in Helicoverpa armigera. Transcriptomic analyses of hemocytes identified an integrin alpha gene (HaINT alpha-PS1) whose expression could be induced by either 20-hydroxyecdysone injection or bead challenge. Isothermal titration calorimetry assays showed that H. armigera CIB1-like (HaCIB1like) weakly bound to the cytoplasmic domain of HaINT alpha-PS1 in the presence of calcium. HaINT alpha-PS1 or HaCIB1-like knockdown inhibited hemocytic encapsulation and phagocytosis, and plasmatocyte spreading. Moreover, HaCIB1-like overexpression in a H. armigera epidermal cell line overexpanded cells and impaired cell phagocytosis. Thus, insect CIB1-like potentially interacted with integrin alpha-cytoplasmic domain and facilitated cell adhesion. This study enriches our understanding of the molecular mechanism underlying integrin-mediated cellular immunity in insects.

Automated summary

This study reveals the interaction between insect CIB1-like and the integrin alpha-cytoplasmic domain, which facilitates cell adhesion. This finding enhances our understanding of the molecular mechanism underlying integrin-mediated cellular immunity in insects.