ENZYME-ACTIVITIES OF LYME-DISEASE AND RELAPSING FEVER BORRELIAE

Activities Of glycosidases (n = 8), esterases (n = 10), arylamidases ( n = 63), acid phosphatase, alkaline phosphatase and phosphoamidase wer e tested in 47 Borrelia strains. Forty-four were B. burgdorferi strain s; 22 of which were isolated from human specimens (skin 13, cerebrospi nal fluid six, and one each from blood, heart muscle and synovia), 13 were isolated from various organs of laboratory animals infected via t ick bite or with human isolates, and nine from ticks. The remaining th ree were the relapsing fever strains B. coriaceae, B. hermsii, and B. turicatae. Strains were of low and high passage but the number of subc ultures did not influence the enzyme patterns obtained by utilization of chromogenic substrates of constitutive enzymes. Glycosidase activit y was absent in almost all strains tested. Esterase activity was high on molecules of chain length less than or equal to 9 carbons. 2-Naphth ylamide derivatives were utilized by strains of human, rodent or tick origin in a range of 66.6 to 83.1%. Almost all strains utilized substr ates for acid and alkaline phosphatase and phosphoamidase. Chymotrypsi n activity was only found in three and two strains from specimens of h uman and rodent origin, respectively; and gamma-glutamyltransferase ac tivity only in three human skin isolates. No strain tested displayed t rypsin activity. Overall, the specific activities of constitutive enzy mes of the Borrelia strains tested are widely similar. Thus, the enzym e profiles did not discriminate between human, animal and tick isolate s, or between human isolates of Borrelia whether cultivated from cereb rospinal fluid or from skin biopsy of Lyme borreliosis patients.