Open AccessApolipophorin III is a substrate for protease IV from Pseudomonas aeruginosa
Author(s) -
Andrejko Mariola,
Cytryńska Małgorzata,
Jakubowicz Teresa
Publication year - 2005
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1016/j.femsle.2004.12.024
Subject(s) - serine protease , protease , galleria mellonella , pseudomonas aeruginosa , microbiology and biotechnology , proteases , biochemistry , serine , biology , hemolymph , enzyme , bacteria , virulence , genetics , gene
Our results demonstrated that Pseudomonas aeruginosa serine protease IV degraded apolipophorin III from the haemolymph of Galleria mellonella larvae. ApoLp‐III protein was degraded in a stepwise manner. Four intermediate forms of 15, 13.3, 11.9 and 9.5 kDa were detected after 30 min digestion while only one of 5.6 kDa was released after 1‐h incubation time. N‐terminal amino acid sequence analysis of 5.6 kDa peptide revealed that it was released from apoLp‐III after cleavage between lysine 70 and 71. ApoLp‐III degradation by protease IV was inhibited by 1 mM TLCK but not 1 mM EDTA, additionally demonstrating that digestion was catalysed by a serine protease. Our data also indicated apoLp‐III degradation in vivo during P. aeruginosa infection of G. mellonella larvae.