DIFFERENCES IN N-ACETYLMURAMYL-L-ALANINE AMIDASE AND LYSOZYME IN SERUM AND CEREBROSPINAL-FLUID OF PATIENTS WITH BACTERIAL-MENINGITIS

N-acetylmuramyl-L-alanine amidase (NAMLAA) specifically degrades pepti doglycan, a major component of bacterial cell walls. Lysozyme degrades peptidoglycan differently by hydrolyzing the aminosugar backbone of p eptidoglycan. In another study, it was shown that the two enzymes act synergistically to inactivate the inflammatory properties of peptidogl ycan, The presence of lysozyme and NAMLAA was determined in serum and cerebrospinal fluid (CSF) of patients with bacterial meningitis. High concentrations of lysozyme were found in CSF while, surprisingly, NAML AA was not present. To explain this phenomenon, the degranulation patt ern of neutrophils in CSF was compared with that of neutrophils from b lood. Specific granules contain lysozyme and the azurophil granules co ntain both lysozyme and NAMLAA. CD66b expression on the cell surface, indicative for fusion of the specific granules with the cell membrane, was higher in CSF than in blood, while the marker for the azurophil g ranules was lower.