A systemic approach to identify non-abundant immunogenic proteins in Lyme disease pathogens.

ABSTRACT: Borrelia burgdorferi, the pathogen of Lyme disease, differentially produces many outer surface proteins (Osp), some of which represent the most abundant membrane proteins, such as OspA, OspB, and OspC. In cultured bacteria, these proteins can account for a substantial fraction of the total cellular or membrane proteins, posing challenges to the identification and analysis of non-abundant proteins, which could serve as novel pathogen detection markers or as vaccine candidates. Herein, we introduced serial mutations to remove these abundant Osps and generated a B. burgdorferi mutant deficient in OspA, OspB, and OspC in an infectious 297-isolate background, designated as Osp^ABC- mutant. Compared to parental isolate, the mutant did not reflect growth

SUBMITTER: Yas OB 

PROVIDER: S-EPMC10805064 | biostudies-literature | 2024 Jan

REPOSITORIES: biostudies-literature