The Expression Levels of Heat Shock Protein 90 (HSP90) in Galleria mellonella Following Infection with the Entomopathogenic Nematode Steinernema carpocapsae and Its Symbiotic Bacteria Xenorhabdus nematophila.

Abstract

Heat shock proteins (HSPs), particularly HSP90, play a vital role in insect responses to environmental and biotic stresses by maintaining protein stability and supporting immune defenses. This study explores HSP90 regulation in Galleria mellonella larvae following exposure to the nematode Steinernema carpocapsae and its symbiotic bacterium Xenorhabdus nematophila. Exposure to live nematodes caused slight changes in HSP90 expression, while non-viable nematodes had no effect, suggesting that nematode secretions or symbiotic bacteria do not directly influence HSP90 levels. However, nematodes with altered surface properties significantly increased HSP90 expression. X. nematophila also moderately elevated HSP90 levels but this effect disappeared when weakly bound surface proteins were removed. Interestingly, under thermal stress, live nematodes reduced heat-induced HSP90 expression, whereas surface-treated nematodes enhanced it. These findings suggest that HSP90 modulation is influenced by biological control agents, highlighting a potential link between HSP90 and immune detection of invaders. This interaction may be crucial in adapting biological control strategies in response to climate change. Further research is needed to clarify HSP activation pathways, host immune interactions, and mechanisms of entomopathogen immune evasion, particularly under varying environmental temperatures, to enhance bioinsecticide efficacy.