2026-10-11T08:33:58Z https://api.figshare.com/v2/oai

oai:figshare.com:article/34026873 2026-09-29T17:38:23Z category_4 category_8 category_13 category_14 category_873 category_46 category_734 category_106 category_132 portal_5 item_type_6 month_year_09_2026

<p>Strain sources.</p> Dan Drecktrah (36180) Laura S. Hall (12206815) Britney Cheff (25138443) Crystal Richards (12206818) Sandra J. Raffel (12240026) Michael Wulf (12206824) Ian T. Bailey (25138446) Frank Gherardini (40103) D. Scott Samuels (12206833) Biochemistry Microbiology Genetics Molecular Biology Chemical Sciences not elsewhere classified Immunology Biological Sciences not elsewhere classified Science Policy Infectious Diseases translation modification system reach high numbers amino acid residues activate carbonyl stress lyme disease spirochete carbonyl stress pathway relapsing fever spirochete div >< p lyme disease spirochetes enigmatic metabolite methylglyoxal burgdorferi mgsa </ carbonyl stress lyme disease relapsing fever mgsa </ burgdorferi </ mayonii </ hermsii </ borreliella </ borrelia </ bb0364 </ significantly reduces results identify relapse phase provide evidence previously believed phosphate imbalance peak level new post necessarily lethal murine infection mouse model metabolic regulation including glycerol dihydroxyacetone phosphate cellular carbohydrate <div><p>The carbonyl stress pathway in bacteria is mediated by the enigmatic metabolite methylglyoxal and is thought to be activated in response to cellular carbohydrate and phosphate imbalance. Methylglyoxal, produced from dihydroxyacetone phosphate by methylglyoxal synthase, covalently modifies nucleophilic groups of amino acid residues, such as lysine, arginine and cysteine, to yield advanced glycation end products. In this work, we have identified several environmental signals, including glycerol and peptides, which activate carbonyl stress in the Lyme disease spirochete <i>Borrelia</i> (<i>Borreliella</i>) <i>burgdorferi</i>. We establish that methylglyoxal production and protein glycation is dependent on the <i>mgsA</i> gene (<i>bb0364</i>) product and show that this pathway is active in Lyme disease spirochetes, but not relapsing fever <i>Borrelia</i> or in <i>B. mayonii</i>. Furthermore, we have investigated the role of carbonyl stress in the tick-mouse model of Lyme disease and provide evidence that production of methylglyoxal and glycation of proteins is not necessarily lethal, as previously believed, at least in Lyme disease spirochetes. Finally, we show that expression of the <i>B. burgdorferi mgsA</i> and carbonyl stress pathway in the relapsing fever spirochete <i>B. hermsii</i> significantly reduces the peak level of spirochetemia during the relapse phase of murine infection. Together, our results identify a new post-translation modification system in Lyme disease spirochetes that appears to be important in governing the lifestyle of this pathogen and seems to be selected against in spirochetes that reach high numbers in the blood.</p></div> 2026-09-29T17:55:00Z Text Journal contribution 10.1371/journal.ppat.1014657.s002 https://figshare.com/articles/journal_contribution/_p_Strain_sources_p_/34026873 CC BY 4.0