Role of serine protease inhibitors in insect-host-pathogen interactions

Serine protease inhibitors (serpins), evolutionary old, structurally conserved molecules, are a superfamily of proteins found in almost all living organisms. Serpins are relatively large, typically 350-500 amino acids in length, with three β-sheets and seven to nine α-helices folding into a conserved tertiary structure with a reactive center loop. Serpins perform various physiological functions in insects, including development, digestion, host-pathogen interactions, and innate immune response. In insects, the innate immune system is characterized as the first and major defense system against the invasion of microorganisms. Serine protease cascades play a critical role in the initiation of innate immune responses, such as melanization and the production of antimicrobial peptides, and are strictly and precisely regulated by serpins. Herein, we provide a microreview on the role of serpins in the insect-host-pathogen interactions, emphasizing their role in immune responses, particularly in diamondback moth (Plutella xylostella), highlighting the important discoveries and also the gaps that remain to be explored in future studies.