{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,1]],"date-time":"2026-10-01T01:41:39Z","timestamp":1790818899712,"version":"4.1.0"},"reference-count":32,"publisher":"American Society for Microbiology","issue":"7","license":[{"start":{"date-parts":[[2009,7,1]],"date-time":"2009-07-01T00:00:00Z","timestamp":1246406400000},"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":["Infect Immun"],"published-print":{"date-parts":[[2009,7]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>\n            HgbA is the sole TonB-dependent receptor for hemoglobin (Hb) acquisition of\n            <jats:italic>Haemophilus ducreyi<\/jats:italic>\n            . Binding of Hb to HgbA is the initial step in heme acquisition from Hb. To better understand this step, we mutagenized\n            <jats:italic>hgbA<\/jats:italic>\n            by deletion of each of the 11 putative surface-exposed loops and expressed each of the mutant proteins in\n            <jats:italic>trans<\/jats:italic>\n            in host strain\n            <jats:italic>H<\/jats:italic>\n            .\n            <jats:italic>ducreyi<\/jats:italic>\n            FX547\n            <jats:italic>hgbA<\/jats:italic>\n            . All mutant proteins were expressed, exported, and detected on the surface by anti-HgbA immunoglobulin G (IgG). Deletion of sequences in loops 5 and 7 of HgbA abolished Hb binding in two different formats. In contrast, HgbA proteins containing deletions in the other nine loops retained the ability to bind Hb. None of the clones expressing mutant proteins were able to grow on plates containing low concentrations of Hb. Previously we demonstrated in a swine model of chancroid infection that an HgbA vaccine conferred complete protection from a challenge infection. Using anti-HgbA IgG from this study and the above deletion mutants, we show that loops 4, 5, and 7 of HgbA were immunogenic and surface exposed and that IgG directed against loops 4 and 5 blocked Hb binding. Furthermore, loop 6 was cleaved by protease on intact\n            <jats:italic>H<\/jats:italic>\n            .\n            <jats:italic>ducreyi<\/jats:italic>\n            , suggesting surface exposure. These data implicate a central domain of HgbA (in respect to the primary amino acid sequence) as important in Hb binding and suggest that this region of the molecule might have potential as a subunit vaccine.\n          <\/jats:p>","DOI":"10.1128\/iai.00034-09","type":"journal-article","created":{"date-parts":[[2009,5,19]],"date-time":"2009-05-19T01:09:49Z","timestamp":1242695389000},"page":"3065-3074","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":14,"title":["An Immunogenic, Surface-Exposed Domain of\n            <i>Haemophilus ducreyi<\/i>\n            Outer Membrane Protein HgbA Is Involved in Hemoglobin Binding"],"prefix":"10.1128","volume":"77","author":[{"given":"Igor","family":"Nepluev","sequence":"first","affiliation":[{"name":"Division of Infectious Diseases, Departments of Medicine"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Galyna","family":"Afonina","sequence":"additional","affiliation":[{"name":"Division of Infectious Diseases, Departments of Medicine"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"William G.","family":"Fusco","sequence":"additional","affiliation":[{"name":"Division of Infectious Diseases, Departments of Medicine"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Isabelle","family":"Leduc","sequence":"additional","affiliation":[{"name":"Division of Infectious Diseases, Departments of Medicine"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Bonnie","family":"Olsen","sequence":"additional","affiliation":[{"name":"Division of Infectious Diseases, Departments of Medicine"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Brenda","family":"Temple","sequence":"additional","affiliation":[{"name":"Biochemistry and Biophysics, University of North Carolina, Chapel Hill, North Carolina 27599"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Christopher","family":"Elkins","sequence":"additional","affiliation":[{"name":"Division of Infectious Diseases, Departments of Medicine"},{"name":"Microbiology and Immunology"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"235","reference":[{"key":"e_1_3_2_2_2","doi-asserted-by":"publisher","DOI":"10.1128\/IAI.74.4.2224-2232.2006"},{"key":"e_1_3_2_3_2","doi-asserted-by":"publisher","DOI":"10.1128\/mr.53.4.377-389.1989"},{"key":"e_1_3_2_4_2","unstructured":"Haemin requirements in Haemophilus with special reference to H. ducreyi 1981"},{"key":"e_1_3_2_5_2","doi-asserted-by":"publisher","DOI":"10.1086\/314483"},{"key":"e_1_3_2_6_2","doi-asserted-by":"publisher","DOI":"10.1086\/315309"},{"key":"e_1_3_2_7_2","doi-asserted-by":"publisher","DOI":"10.1128\/IAI.70.11.5955-5964.2002"},{"key":"e_1_3_2_8_2","doi-asserted-by":"publisher","DOI":"10.1128\/IAI.68.12.6988-6996.2000"},{"key":"e_1_3_2_9_2","doi-asserted-by":"publisher","DOI":"10.1128\/IAI.66.3.987-993.1998"},{"key":"e_1_3_2_10_2","doi-asserted-by":"publisher","DOI":"10.1128\/IAI.68.7.4092-4101.2000"},{"key":"e_1_3_2_11_2","doi-asserted-by":"publisher","DOI":"10.1128\/IAI.67.7.3317-3328.1999"},{"key":"e_1_3_2_12_2","doi-asserted-by":"publisher","DOI":"10.1128\/iai.63.4.1241-1245.1995"},{"key":"e_1_3_2_13_2","doi-asserted-by":"publisher","DOI":"10.1111\/j.1365-2958.1994.tb01339.x"},{"key":"e_1_3_2_14_2","doi-asserted-by":"publisher","DOI":"10.1128\/iai.63.6.2194-2200.1995"},{"key":"e_1_3_2_15_2","doi-asserted-by":"publisher","DOI":"10.1128\/IAI.66.1.151-160.1998"},{"key":"e_1_3_2_16_2","doi-asserted-by":"publisher","DOI":"10.1128\/JCM.38.4.1520-1526.2000"},{"key":"e_1_3_2_17_2","doi-asserted-by":"publisher","DOI":"10.1128\/jcm.7.1.39-43.1978"},{"key":"e_1_3_2_18_2","doi-asserted-by":"publisher","DOI":"10.1002\/pro.5560030505"},{"key":"e_1_3_2_19_2","doi-asserted-by":"publisher","DOI":"10.1086\/586901"},{"key":"e_1_3_2_20_2","doi-asserted-by":"publisher","DOI":"10.1128\/IAI.72.6.3418-3428.2004"},{"key":"e_1_3_2_21_2","doi-asserted-by":"publisher","DOI":"10.3109\/10408419209114559"},{"key":"e_1_3_2_22_2","doi-asserted-by":"publisher","DOI":"10.1128\/JCM.40.10.3694-3702.2002"},{"key":"e_1_3_2_23_2","doi-asserted-by":"publisher","DOI":"10.1099\/mic.0.26448-0"},{"key":"e_1_3_2_24_2","doi-asserted-by":"publisher","DOI":"10.1093\/infdis\/163.2.233"},{"key":"e_1_3_2_25_2","doi-asserted-by":"publisher","DOI":"10.1128\/JB.181.18.5865-5870.1999"},{"key":"e_1_3_2_26_2","doi-asserted-by":"publisher","DOI":"10.1128\/JB.181.7.2067-2074.1999"},{"key":"e_1_3_2_27_2","unstructured":"Reference deleted."},{"key":"e_1_3_2_28_2","first-page":"818","volume":"79","year":"2001","unstructured":"Steen, R. 2001. Eradicating chancroid. Bull. W. H. O.79:818-826.","journal-title":"Bull. W. H. 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