The major outer surface proteins of Lyme disease spirochaetes are differentially expressed in different isolates. strain F1 expresses none, or very low amounts, of the OspA and OspB proteins. To elucidate the mechanisms that control the expression of these abundant surface proteins the operon of F1 was cloned, sequenced and compared to the previously sequenced operon of ACAI and B31. The two strains showed almost 100% identity at the DNA level, although Coomassie-stained gels and Western blot analyses showed significant variation in the Osp protein content. Transcriptional analysis revealed that the amount of mRNA produced in F1 varies more than the amount of protein, suggesting that the expression of OspA and OspB proteins is regulated at both the transcriptional and the translational level. Furthermore, the inverse relationship between the transcription of and the operon could indicate coregulation of these separately encoded operons.


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