<HashMap><database>bioimages</database><scores/><additional><omics_type>Unknown</omics_type><submitter/><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-BIAD1573</full_dataset_link><repository>bioimages</repository><figure_sub>Specimen</figure_sub><figure_sub>Image analysis</figure_sub><figure_sub>Funding</figure_sub><figure_sub>Study Component</figure_sub><figure_sub>organisation</figure_sub><figure_sub>Biosample</figure_sub><figure_sub>Associations</figure_sub><figure_sub>Image acquisition</figure_sub><pubmed_authors>Joshua W. McCausland</pubmed_authors><pubmed_authors>Christine Jacobs-Wagner</pubmed_authors><pubmed_authors>CJW lab</pubmed_authors></additional><is_claimable>false</is_claimable><name>Bacterial and host enzymes modulate the inflammatory response produced by the peptidoglycan of the Lyme disease agent</name><description>The spirochete Borrelia burgdorferi causes Lyme disease. In some patients, an excessive, dysregulated proinflammatory immune response can develop in joints leading to persistent arthritis. In such patients, persistence of antigenic B. burgdorferi peptidoglycan (PGBb) fragments within joint tissues may contribute to the immunopatho-genesis, even after appropriate antibiotic treatment. In live B. burgdorferi cells, the outer membrane shields the polymeric PGBb sacculus from exposure to the immune system. However, unlike most diderm bacteria, B. burgdorferi releases PGBb turnover products into its environment due to the absence of recycling activity. In this study, we identified the released PGBb fragments using a mass spectrometry-based approach. By characterizing the L,D-carboxypeptidase ac</description><dates><release>2025-01-11T00:00:00Z</release><modification>2025-01-20T13:19:41.008Z</modification><creation>2025-01-10T23:53:35.516Z</creation></dates><accession>S-BIAD1573</accession><cross_references/></HashMap>