{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,25]],"date-time":"2026-09-25T06:04:03Z","timestamp":1790316243434,"version":"4.1.0"},"reference-count":69,"publisher":"Microbiology Society","issue":"12","license":[{"start":{"date-parts":[[2021,12,1]],"date-time":"2021-12-01T00:00:00Z","timestamp":1638316800000},"content-version":"unspecified","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/100010796","name":"Azm and Saade Association","doi-asserted-by":"crossref","id":[{"id":"10.13039\/100010796","id-type":"DOI","asserted-by":"crossref"}]},{"name":"Lebanese Association for Scientific Research"},{"name":"Fondation Universitaire Rabelais"},{"name":"INRAE- International Mobility Service"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2021,12,1]]},"abstract":"<jats:p>Polyamines constitute a group of organic polycations positively charged at physiological pH. They are involved in a large variety of biological processes, including the protection against physiological stress. In this study, we show that the genome of <jats:italic>\n                     <jats:named-content content-type=\"species\">\n                        <jats:ext-link xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" ext-link-type=\"uri\" xlink:href=\"http:\/\/doi.org\/10.1601\/nm.5609\" xlink:type=\"simple\">Streptococcus agalactiae<\/jats:ext-link>\n                     <\/jats:named-content>\n                  <\/jats:italic>, a commensal bacterium of the intestine and the vagina and one of the most common agents responsible of neonate infections, does not encode proteins homologous to the specific enzymes involved in the known polyamine synthetic pathways. This lack of biosynthetic capability was verified experimentally by TLC analysis of the intracellular content of <jats:italic>\n                     <jats:named-content content-type=\"species\">\n                        <jats:ext-link xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" ext-link-type=\"uri\" xlink:href=\"http:\/\/doi.org\/10.1601\/nm.5609\" xlink:type=\"simple\">S. agalactiae<\/jats:ext-link>\n                     <\/jats:named-content>\n                  <\/jats:italic> grown in the absence of polyamines. However, similar analyses showed that the polyamines spermidine, spermine and putrescine can be imported from the growth media into the bacteria. We found that all strains of <jats:italic>\n                     <jats:named-content content-type=\"species\">\n                        <jats:ext-link xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" ext-link-type=\"uri\" xlink:href=\"http:\/\/doi.org\/10.1601\/nm.5609\" xlink:type=\"simple\">S. agalactiae<\/jats:ext-link>\n                     <\/jats:named-content>\n                  <\/jats:italic> possess the genes encoding the polyamine ABC transporter PotABCD. We demonstrated that these genes form an operon with <jats:italic>folK<\/jats:italic>, a gene involved in folate biosynthesis, <jats:italic>murB<\/jats:italic>, a gene involved in peptidoglycan biosynthesis, and with <jats:italic>clc<\/jats:italic>, a gene encoding a Cl<jats:sup>\u2212<\/jats:sup>\/H<jats:sup>+<\/jats:sup> antiporter involved in resistance to acid stress in <jats:italic>\n                     <jats:named-content content-type=\"species\">\n                        <jats:ext-link xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" ext-link-type=\"uri\" xlink:href=\"http:\/\/doi.org\/10.1601\/nm.3093\" xlink:type=\"simple\">Escherichia coli<\/jats:ext-link>\n                     <\/jats:named-content>\n                  <\/jats:italic>. Transcription of the <jats:italic>potABCD<\/jats:italic> operon is induced by peroxide-induced oxidative stress but not by acidic stress. Spermidine and spermine were found to be inducers of <jats:italic>potABCD<\/jats:italic> transcription at pH 7.4 whereas putrescine induces this expression only during peroxide-induced oxidative stress. Using a deletion mutant of <jats:italic>potABCD<\/jats:italic>, we were nevertheless unable to associate phenotypic traits to the PotABCD transporter, probably due to the existence of one or more as yet identified transporters with a redundant action.<\/jats:p>","DOI":"10.1099\/mic.0.001124","type":"journal-article","created":{"date-parts":[[2021,12,15]],"date-time":"2021-12-15T18:15:36Z","timestamp":1639592136000},"source":"Crossref","is-referenced-by-count":8,"title":["Investigation of the polyamine biosynthetic and transport capability of Streptococcus agalactiae: the non-essential PotABCD transporter"],"prefix":"10.1099","volume":"167","author":[{"given":"Sarah","family":"Khazaal","sequence":"first","affiliation":[{"name":"Azm Center for Research in Biotechnology and its Applications, LBA3B, EDST, Lebanese University, Tripoli, 1300, Lebanon"},{"name":"ISP, Bact\u00e9ries et Risque Materno-Foetal, Universit\u00e9 de Tours, INRAE, 37032 Tours, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Rim","family":"Al Safadi","sequence":"additional","affiliation":[{"name":"Azm Center for Research in Biotechnology and its Applications, LBA3B, EDST, Lebanese University, Tripoli, 1300, Lebanon"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-3880-3098","authenticated-orcid":false,"given":"Dani","family":"Osman","sequence":"additional","affiliation":[{"name":"Azm Center for Research in Biotechnology and its Applications, LBA3B, EDST, Lebanese University, Tripoli, 1300, Lebanon"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Aur\u00e9lia","family":"Hiron","sequence":"additional","affiliation":[{"name":"ISP, Bact\u00e9ries et Risque Materno-Foetal, Universit\u00e9 de Tours, INRAE, 37032 Tours, 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