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The canonical ATP-dependent protease Lon participates in an assortment of biological processes in bacteria, including the catalysis of damaged or senescent proteins and short-lived regulatory proteins.  Borrelia  spirochetes are unusual in that they code for two putative ATP-dependent Lon homologs, Lon-1 and Lon-2.  Borrelia burgdorferi , the etiologic agent of Lyme disease, is transmitted through the blood feeding of  Ixodes  ticks. Previous work in our laboratory reported that  B. burgdorferi lon-1  is upregulated transcriptionally by exposure to blood  in vitro , while  lon-2  is not. Because blood induction of Lon-1 may be of importance in the regulation of virulence factors critical for spirochete transmission, the clarification of functional roles for these two proteases in  B. burgdorferi  was the object of this study. On the chromosome,  lon-2  is immediately downstream of ATP-dependent proteases  clpP  and  clpX , an arrangement identical to that of  lon  of  Escherichia coli . Phylogenetic analysis revealed that Lon-1 and Lon-2 cluster separately due to differences in the NH 2 -terminal substrate binding domains that may reflect differences in substrate specificity. Recombinant Lon-1 manifested properties of an ATP-dependent chaperone-protease  in vitro  but did not complement an  E. coli  Lon mutant, while Lon-2 corrected two characteristic Lon-mutant phenotypes. We conclude that  B. burgdorferi  Lons -1 and -2 have distinct functional roles. Lon-2 functions in a manner consistent with canonical Lon, engaged in cellular homeostasis. Lon-1, by virtue of its blood induction, and as a unique feature of the Borreliae, may be important in host adaptation from the arthropod to a warm-blooded host.

Evidence That Two ATP-Dependent (Lon) Proteases in Borrelia burgdorferi Serve Different Functions