{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,2]],"date-time":"2026-10-02T23:58:44Z","timestamp":1790985524294,"version":"4.1.0"},"reference-count":83,"publisher":"Wiley","issue":"6","license":[{"start":{"date-parts":[[2011,5,6]],"date-time":"2011-05-06T00:00:00Z","timestamp":1304640000000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Molecular Microbiology"],"published-print":{"date-parts":[[2011,6]]},"abstract":"<jats:title>Summary<\/jats:title><jats:p>We studied three Fur\u2010regulated systems of <jats:italic>Listeria monocytogenes<\/jats:italic>: the <jats:italic>srtB<\/jats:italic> region, that encodes sortase\u2010anchored proteins and a putative ABC transporter, and the <jats:italic>fhu<\/jats:italic> and <jats:italic>hup<\/jats:italic> operons, that produce putative ABC transporters for ferric hydroxamates and haemin (Hn)\/haemoglobin (Hb) respectively. Deletion of <jats:italic>lmo2185<\/jats:italic> in the <jats:italic>srtB<\/jats:italic> region reduced listerial [<jats:sup>59<\/jats:sup>Fe]\u2010Hn transport, and purified Lmo2185 bound [<jats:sup>59<\/jats:sup>Fe]\u2010Hn (<jats:italic>K<\/jats:italic><jats:sub>D<\/jats:sub>\u2003=\u200312\u2003nM), leading to its designation as a <jats:styled-content>H<\/jats:styled-content>n\/<jats:styled-content>H<\/jats:styled-content>b <jats:styled-content>b<\/jats:styled-content>inding <jats:styled-content>p<\/jats:styled-content>rotein (<jats:italic>hbp2<\/jats:italic>)<jats:italic>.<\/jats:italic> Purified Hbp2 also acted as a haemophore, capturing and supplying Hn from the environment. Nevertheless, Hbp2 only functioned in [<jats:sup>59<\/jats:sup>Fe]\u2010Hn transport at external concentrations less than 50\u2003nM: at higher Hn levels its uptake occurred with equivalent affinity and rate without Hbp2. Similarly, deletion of sortase A had no effect on ferric siderophore or Hn\/Hb transport at any concentration, and the <jats:italic>srtA<\/jats:italic>\u2010independence of listerial Hn\/Hb uptake distinguished it from comparable systems of <jats:italic>Staphylococcus aureus.<\/jats:italic> In the cytoplasmic membrane, the Hup transporter was specific for Hn: its lipoprotein (HupD) only showed high affinity for the iron porphyrin (<jats:italic>K<\/jats:italic><jats:sub>D<\/jats:sub>\u2003=\u200326\u2003nM). Conversely, the FhuD lipoprotein encoded by the <jats:italic>fhu<\/jats:italic> operon had broad specificity: it bound both ferric siderophores and Hn, with the highest affinity for ferrioxamine B (<jats:italic>K<\/jats:italic><jats:sub>D<\/jats:sub>\u2003=\u2003123\u2003nM). Deletions of Hup permease components <jats:italic>hupD<\/jats:italic>, <jats:italic>hupG<\/jats:italic> or <jats:italic>hupDGC<\/jats:italic> reduced Hn\/Hb uptake, and complementation of <jats:italic>\u0394hupC<\/jats:italic> and <jats:italic>\u0394hupG<\/jats:italic> by chromosomal integration of <jats:italic>hupC<\/jats:italic><jats:sup>+<\/jats:sup> and <jats:italic>hupG<\/jats:italic><jats:sup>+<\/jats:sup> alleles on pPL2 restored growth promotion by Hn\/Hb. However, <jats:italic>\u0394hupDGC<\/jats:italic> did not completely eliminate [<jats:sup>59<\/jats:sup>Fe]\u2010Hn transport, implying the existence of another cytoplasmic membrane Hn transporter. The overall <jats:italic>K<\/jats:italic><jats:sub>M<\/jats:sub> of Hn uptake by wild\u2010type strain EGD\u2010e was 1\u2003nM, and it occurred at similar rates (<jats:italic>V<\/jats:italic><jats:sub>max<\/jats:sub>\u2003=\u200323\u2003pmol\u200310<jats:sup>9<\/jats:sup> cells<jats:sup>\u22121<\/jats:sup>\u2003min<jats:sup>\u22121<\/jats:sup>) to those of ferric siderophore transporters. In the <jats:italic>\u0394hupDGC<\/jats:italic> strain uptake occurred at a threefold lower rate (<jats:italic>V<\/jats:italic><jats:sub>max<\/jats:sub>\u2003=\u20037\u2003pmol\u200310<jats:sup>9<\/jats:sup> cells<jats:sup>\u22121<\/jats:sup>\u2003min<jats:sup>\u22121<\/jats:sup>). The results show that at low (&lt;\u200350\u2003nM) levels of Hn, SrtB\u2010dependent peptidoglycan\u2010anchored proteins (e.g. Hbp2) bind the porphyrin, and HupDGC or another transporter completes its uptake into the cytoplasm. However, at higher concentrations Hn uptake is SrtB\u2010independent: peptidoglycan\u2010anchored binding proteins are dispensable because HupDGC directly absorbs and internalizes Hn. Finally, <jats:italic>\u0394hupDGC<\/jats:italic> increased the LD<jats:sub>50<\/jats:sub> of <jats:italic>L. monocytogenes<\/jats:italic> 100\u2010fold in the mouse infection model, reiterating the importance of this system in listerial virulence.<\/jats:p>","DOI":"10.1111\/j.1365-2958.2011.07667.x","type":"journal-article","created":{"date-parts":[[2011,5,6]],"date-time":"2011-05-06T07:21:07Z","timestamp":1304666467000},"page":"1581-1597","source":"Crossref","is-referenced-by-count":51,"title":["Sortase independent and dependent systems for acquisition of haem and haemoglobin in <i>Listeria monocytogenes<\/i>"],"prefix":"10.1111","volume":"80","author":[{"given":"Qiaobin","family":"Xiao","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Xiaoxu","family":"Jiang","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kyle 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