Mc. Guardati et al., THE USE OF MONOCLONAL-ANTIBODIES FOR STUDYING THE BIOLOGICAL PROPERTIES OF STAPHYLOCOCCUS-AUREUS ENDO-BETA-N-ACETYLGLUCOSAMINIDASE, FEMS microbiology letters, 112(1), 1993, pp. 73-79
Staphylococcus aureus endo-beta-N-acetylglucosaminidase (SaG) has been
suggested to function as a virulence determinant which interferes wit
h the host cellular immune response. To further characterize the biolo
gical properties of SaG, monoclonal antibodies (mAbs) were raised agai
nst purified SaG. Four IgG1 subclass mAbs were obtained, none of which
reacted with the reduced, sodium dodecyl sulphate pretreated or boile
d enzyme. The ability of the mAbs to react with the enzymes present in
supernatants obtained from 197 S. aureus strains indicated that they
recognized epitopes which are highly conserved; bacteriolytic enzymes
produced by staphylococci other than S. aureus did not show any cross-
reactivity. After pretreatment of SaG with mAbs (mAb-SaG molar ratios
varying from 1 to 20), it was shown that all selected mAbs caused, at
a mAb: SaG molar ratio of 10, a 90% inhibition of SaG bacteriolytic ac
tivity and a statistically significant reduction of its ability to int
erfere with phagocytosis by human polymorphonuclear leukocytes. All se
lected mAbs reacted with several commercially available exo-beta-N-ace
tylglucosaminidases; mAb C1/10-11 also reacted with chicken and turkey
egg muramidases and, at a mAb:SaG molar ratio of 10, inhibited their
bacteriolytic activity by 97%. This suggests that one or more epitopes
present in the above exo-glucosaminidases and muramidases share some
degree of homology with others present in SaG.