Lyme Disease Borreliae Research Articles

Relationship between infectivity and OspC expression in Lyme diseaseBorrelia

Borrelia burgdorferi sensu stricto strain 297 and B. garinii strains HP1 and 12-92 were serially subcultured for 36-50 passages in vitro for 1 year. All low-passage strains showed abundant expression of outer surface protein C (OspC) in the 22-23-kDa range, but the high-passage strains lost or showed reduced expression of OspC in comparison with the low-passage strains. The low-passage strains efficiently infected outbred ddY mice when inoculated into the hind footpad or peritoneal cavity. In contrast, the incidence of infection with the high-passage strains was low. Isolates from the bladders of mice inoculated with the high-passage strains expressed large amounts of OspC in comparison with those originally inoculated. These results indicate that OspC expression is related to the infectivity of Lyme disease borreliae.

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 were tested in 47 Borrelia strains. Forty-four were B. burgdorferi strains; 22 of which were isolated from human specimens (skin 13, cerebrospinal fluid six, and one each from blood, heart muscle and synovia), 13 were isolated from various organs of laboratory animals infected via tick bite or with human isolates, and nine from ticks. The remaining three were the relapsing fever strains B. coriaceae, B. hermsii, and B. turicatae. Strains were of low and high passage but the number of subcultures did not influence the enzyme patterns obtained by utilization of chromogenic substrates of constitutive enzymes. Glycosidase activity was absent in almost all strains tested. Esterase activity was high on molecules of chain length 9 carbons. 2-Naphthylamide derivatives were utilized by strains of human, rodent or tick origin in a range of 66.6 to 83.1%. Almost all strains utilized substrates for acid and alkaline phosphatase and phosphoamidase. Chymotrypsin activity was only found in three and two strains from specimens of human and rodent origin, respectively; and γ-glutamyltransferase activity only in three human skin isolates. No strain tested displayed trypsin activity. Overall, the specific activities of constitutive enzymes of the Borrelia strains tested are widely similar. Thus, the enzyme profiles did not discriminate between human, animal and tick isolates, or between human isolates of Borrelia whether cultivated from cerebrospinal fluid or from skin biopsy of Lyme borreliosis patients.

Serological distinction between syphilis and Lyme borreliosis

The serological distinction of an immune response to the agent of syphilis, Treponema (T.) pallidum, and Lyme disease borreliae is difficult due to the existence of cross-reacting antibodies. In this study, the immunoblot technique is used to compare the immune response of sera from patients with syphilis or Lyme borreliosis to either T. pallidum or Borrelia (B.) burgdorferi. Patients with syphilis showed an IgG response to the 17 and 15 kDa antigens of T. pallidum, whereas sera from patients with Lyme borreliosis-especially in late stages of the disease-reacted with the 95 and 19-17 kDa antigens of B. burgdorferi. Thus, IgG antibodies against low molecular weight antigens of T. pallidum (17, 15 kDa) or B. burgdorferi (19-17 kDa) may represent useful markers for the serological diagnosis of syphilis or Lyme borreliosis.

Polymorphisms of major surface proteins of Borrelia burgdorferi

Forty-five isolates of Borrelia burgdorferi, the etiologic agent of Lyme disease, were examined with monoclonal antibodies directed against the surface proteins, OspA and OspB. Eighteen of 21 strains of European origin could be distinguished from 24 North American strains on the basis of their reactivities with two antibodies, one specific for an OspA protein and one specific for an OspB protein. Differences in antibody reactivities were associated with differences in the electrophoretic migrations of OspA and OspB proteins. Thus, Lyme disease borreliae are polymorphic with respect to their major surface proteins. The demonstrated distinctions between the majorities of European and North American strains may have relevance for both epidemiologic and pathogenic studies of Lyme disease.

Heterogeneity of Major Proteins in Lyme Disease Borreliae: A Molecular Analysis of North American and European Isolates

We examined 46 isolates of Borrelia burgdorferi, the etiologic agent of Lyme disease and related disorders, with polyacrylamide gel electrophoresis and monoclonal antibodies. Our attention was on the OspA proteins, which are major proteins of the spirochete. There were at least four discernible phenotypes of the OspA protein. While 25 North American isolates were, with one exception, homogeneous in the type of OspA protein that they produced, 21 European isolates were heterogeneous in the types of OspA proteins represented. Only three European strains resembled North American strains in their OspA phenotype. Application of a deoxyribonucleic acid probe for an ospA gene demonstrated that the arrangement of ospA-associated sequences in the DNA differed between isolates.