Apolipophorin III is a substrate for protease IV from Pseudomonas aeruginosa |
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Authors: | Andrejko Mariola Cytryńska Małgorzata Jakubowicz Teresa |
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Affiliation: | Department of Basic and Applied Biology, Faculty of Biotechnology and Faculty of Sciences, University of L'Aquila, Via Vetoio 1, Località Coppito, I-67010 L'Aquila, Italy. poma@univaq.it |
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Abstract: | 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. |
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Keywords: | Apolipophorin III Galleria mellonella Protease IV Pseudomonas aeruginosa |
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