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Recent studies have uncovered both heme (<jats:italic>isd<\/jats:italic>) and siderophore-mediated (<jats:italic>asb<\/jats:italic>) iron transport pathways in this pathogen. Whereas deletion of the<jats:italic>asb<\/jats:italic>genes results in reduced virulence, the loss of three surface components from<jats:italic>isd<\/jats:italic>had no effect, thereby leaving open the question of what additional factors in<jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">B. anthracis<\/jats:named-content>are responsible for iron uptake from the most abundant iron source for mammals, heme. Here, we describe the first functional characterization of<jats:italic>bas0520<\/jats:italic>, a gene recently implicated in anthrax disease progression.<jats:italic>bas0520<\/jats:italic>encodes a single near-iron transporter (NEAT) domain and several leucine-rich repeats. The NEAT domain binds heme, despite lacking a stabilizing tyrosine common to the NEAT superfamily of hemoproteins. The NEAT domain also binds hemoglobin and can acquire heme from hemoglobin in solution. Finally, deletion of<jats:italic>bas0520<\/jats:italic>resulted in bacilli unable to grow efficiently on heme or hemoglobin as an iron source and yielded the most significant phenotype relative to that for other putative heme uptake systems, a result that suggests that this protein plays a prominent role in the replication of<jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">B. anthracis<\/jats:named-content>in hematogenous environments. Thus, we have assigned the name of Hal (<jats:underline>h<\/jats:underline>eme-<jats:underline>a<\/jats:underline>cquisition<jats:underline>l<\/jats:underline>eucine-rich repeat protein) to BAS0520. These studies advance our understanding of heme acquisition by this dangerous pathogen and justify efforts to determine the mechanistic function of this novel protein for vaccine or inhibitor development.<\/jats:p>","DOI":"10.1128\/jb.00685-12","type":"journal-article","created":{"date-parts":[[2012,8,4]],"date-time":"2012-08-04T02:59:35Z","timestamp":1344049175000},"page":"5513-5521","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":39,"title":["Hal Is a Bacillus anthracis Heme Acquisition Protein"],"prefix":"10.1128","volume":"194","author":[{"given":"Miriam A.","family":"Balderas","sequence":"first","affiliation":[{"name":"Department of Molecular Virology and Microbiology, Baylor College of Medicine, Houston, Texas, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Christopher L.","family":"Nobles","sequence":"additional","affiliation":[{"name":"Department of Molecular Virology and Microbiology, Baylor College of Medicine, Houston, Texas, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Erin S.","family":"Honsa","sequence":"additional","affiliation":[{"name":"Department of Molecular Virology and Microbiology, Baylor College of Medicine, Houston, Texas, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Embriette R.","family":"Alicki","sequence":"additional","affiliation":[{"name":"Interdepartmental Program in Cell and Molecular Biology, Baylor College of Medicine, Houston, Texas, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Anthony W.","family":"Maresso","sequence":"additional","affiliation":[{"name":"Department of Molecular Virology and Microbiology, Baylor College of Medicine, Houston, Texas, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"235","reference":[{"key":"e_1_3_2_2_2","doi-asserted-by":"crossref","first-page":"940","DOI":"10.1016\/S1357-2725(01)00063-2","article-title":"Chemistry and biology of eukaryotic iron metabolism","volume":"33","author":"Aisen P","year":"2001","unstructured":"AisenP EnnsC Wessling-ResnickM. 2001. 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