Antibacterial non-glycosidase activity of invertebrate destabilase-lysozyme and of its helical amphipathic peptides.
BACKGROUND
Since bactericidal properties of some lysozymes are independent of their glycosidase activity, we have investigated this phenomenon for destabilase-lysozyme (DL) from medicinal leech (Hirudo medicinalis).


METHODS
Glycosidase activity was determined on Micrococcus luteus, non-enzymatic antibacterial activity of heat-treated DL and of synthetic peptides alpha1, alpha2 and alpha3 (fragments of its primary structure) on M. luteus, Escherichia coli, Bacillus brevis and Streptomyces chrysomallus.


RESULTS
Glycosidase activity disappeared after the heating of native DL at 100 degrees C for 40 min. Antibacterial activity of heat-treated DL for M. luteus MDMSU128 and MDMSU140 expressed as minimal inhibitory concentration was 9.8.10(-8) and 12.10(-8) M, respectively, and to E. coli MDMSU52 11.10(-8) M. Antibacterial activity of synthetic peptide alpha1 for M. luteus MDMSU128 and for E. coli MDMSU52 was 8.3.10(-5) and 4.9.10(-5) M, respectively.


CONCLUSIONS
DL is the first invertebrate lysozyme with combined enzymatic and non-enzymatic antibacterial action.
Zavalova
L L
LL
Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow. saliva1@yandex.ru
Yudina
T G
TG
Artamonova
I I
II
Baskova
I P
IP
D000818:Animals; D000890:Anti-Infective Agents / Q000302:isolation & purification / Q000494:pharmacology*; D001419:Bacteria / Q000187:drug effects* / Q000201:enzymology; D010450:Endopeptidases / Q000302:isolation & purification / Q000494:pharmacology*; D006026:Glycoside Hydrolases / Q000378:metabolism; D047709:Hirudo medicinalis / Q000201:enzymology*; D008826:Microbial Sensitivity Tests; D010446:Peptide Fragments / Q000494:pharmacology*
D000890:Anti-Infective Agents; D010446:Peptide Fragments; D006026:Glycoside Hydrolases; D010450:Endopeptidases; C045348:fibrin destabilase