{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,30]],"date-time":"2026-09-30T05:17:41Z","timestamp":1790745461830,"version":"4.1.0"},"reference-count":50,"publisher":"American Society for Microbiology","issue":"4","license":[{"start":{"date-parts":[[2003,2,15]],"date-time":"2003-02-15T00:00:00Z","timestamp":1045267200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.asm.org\/non-commercial-tdm-license"}],"content-domain":{"domain":["journals.asm.org"],"crossmark-restriction":true},"short-container-title":["J Bacteriol"],"published-print":{"date-parts":[[2003,2,15]]},"abstract":"<jats:title>ABSTRACT<\/jats:title><jats:p>Relapsing-fever spirochetes achieve high cell densities (&gt;10<jats:sup>8<\/jats:sup>\/ml) in their host's blood, while Lyme disease spirochetes do not (&lt;10<jats:sup>5<\/jats:sup>\/ml). This striking contrast in pathogenicity of these two groups of bacteria suggests a fundamental difference in their ability to either exploit or survive in blood.<jats:italic>Borrelia hermsii,<\/jats:italic>a tick-borne relapsing-fever spirochete, contains orthologs to<jats:italic>glpQ<\/jats:italic>and<jats:italic>glpT,<\/jats:italic>genes that encode glycerophosphodiester phosphodiesterase (GlpQ) and glycerol-3-phosphate transporter (GlpT), respectively. In other bacteria, GlpQ hydrolyzes deacylated phospholipids to glycerol-3-phosphate (G3P) while GlpT transports G3P into the cytoplasm. Enzyme assays on 17 isolates of borreliae demonstrated GlpQ activity in relapsing-fever spirochetes but not in Lyme disease spirochetes. Southern blots demonstrated<jats:italic>glpQ<\/jats:italic>and<jats:italic>glpT<\/jats:italic>in all relapsing-fever spirochetes but not in the Lyme disease group. A Lyme disease spirochete,<jats:italic>Borrelia burgdorferi,<\/jats:italic>that was transformed with a shuttle vector containing<jats:italic>glpTQ<\/jats:italic>from<jats:italic>B. hermsii<\/jats:italic>produced active enzyme, which demonstrated the association of<jats:italic>glpQ<\/jats:italic>with the hydrolysis of phospholipids. Sequence analysis of<jats:italic>B. hermsii<\/jats:italic>identified<jats:italic>glpF, glpK,<\/jats:italic>and<jats:italic>glpA,<\/jats:italic>which encode the glycerol facilitator, glycerol kinase, and glycerol-3-phosphate dehydrogenase, respectively, all of which are present in<jats:italic>B. burgdorferi.<\/jats:italic>All spirochetes examined had<jats:italic>gpsA,<\/jats:italic>which encodes the enzyme that reduces dihydroxyacetone phosphate (DHAP) to G3P. Consequently, three pathways for the acquisition of G3P exist among borreliae: (i) hydrolysis of deacylated phospholipids, (ii) reduction of DHAP, and (iii) uptake and phosphorylation of glycerol. The unique ability of relapsing-fever spirochetes to hydrolyze phospholipids may contribute to their higher cell densities in blood than those of Lyme disease spirochetes.<\/jats:p>","DOI":"10.1128\/jb.185.4.1346-1356.2003","type":"journal-article","created":{"date-parts":[[2003,1,31]],"date-time":"2003-01-31T20:03:10Z","timestamp":1044043390000},"page":"1346-1356","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":69,"title":["Glycerol-3-Phosphate Acquisition in Spirochetes: Distribution and Biological Activity of Glycerophosphodiester Phosphodiesterase (GlpQ) among<i>Borrelia<\/i>Species"],"prefix":"10.1128","volume":"185","author":[{"given":"Tom G.","family":"Schwan","sequence":"first","affiliation":[{"name":"Laboratory of Human Bacterial Pathogenesis"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"James M.","family":"Battisti","sequence":"additional","affiliation":[{"name":"Laboratory of Human Bacterial Pathogenesis"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Stephen F.","family":"Porcella","sequence":"additional","affiliation":[{"name":"Laboratory of Human Bacterial Pathogenesis"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sandra J.","family":"Raffel","sequence":"additional","affiliation":[{"name":"Laboratory of Human Bacterial Pathogenesis"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Merry E.","family":"Schrumpf","sequence":"additional","affiliation":[{"name":"Laboratory of Human Bacterial Pathogenesis"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Elizabeth R.","family":"Fischer","sequence":"additional","affiliation":[{"name":"Rocky Mountain Laboratories Microscopy Branch, Rocky Mountain Laboratories, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Hamilton, Montana 59840"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"James A.","family":"Carroll","sequence":"additional","affiliation":[{"name":"Rocky Mountain Laboratories Microscopy Branch, Rocky Mountain Laboratories, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Hamilton, Montana 59840"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Philip E.","family":"Stewart","sequence":"additional","affiliation":[{"name":"Laboratory of Human Bacterial Pathogenesis"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Patricia","family":"Rosa","sequence":"additional","affiliation":[{"name":"Laboratory of Human Bacterial Pathogenesis"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Greg A.","family":"Somerville","sequence":"additional","affiliation":[{"name":"Laboratory of Human Bacterial Pathogenesis"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"235","reference":[{"key":"e_1_3_2_2_2","doi-asserted-by":"publisher","DOI":"10.1128\/mr.50.4.381-400.1986"},{"key":"e_1_3_2_3_2","doi-asserted-by":"crossref","first-page":"403","DOI":"10.1093\/infdis\/173.2.403","volume":"173","year":"1996","unstructured":"Barbour, A. 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