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Susceptibility of proteins and peptides present in immune hemolymph of Galleria mellonella Fabricius (Lepidoptera: Pyralidae) larvae to proteolytic degradation by purified elastase B of Pseudomonas aeruginosa was studied. Results showed that apoLp-III protein was gradually digested by elastase B in vitro. Additionally, polipeptides with molecular mass 6.5 and 4 kDa were degraded after treatment with the studied enzyme. The lack of these peptides and the decrease in anti-Escherichia coli activity could indicate that inducible antimicrobial peptides were digested by elastase B. On the contrary, no change in the lysosome activity level was observed in immune hemolymph incubated with elastase B. Thus, elastase B might contribute to the pathogenesis of P. aeruginosa.