{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,7,30]],"date-time":"2025-07-30T13:35:16Z","timestamp":1753882516155,"version":"3.41.2"},"reference-count":35,"publisher":"American Society for Microbiology","issue":"5","license":[{"start":{"date-parts":[[2025,5,13]],"date-time":"2025-05-13T00:00:00Z","timestamp":1747094400000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"},{"start":{"date-parts":[[2025,5,13]],"date-time":"2025-05-13T00:00:00Z","timestamp":1747094400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.asm.org\/non-commercial-tdm-license"}],"funder":[{"DOI":"10.13039\/100000060","name":"National Institute of Allergy and Infectious Diseases","doi-asserted-by":"publisher","award":["R01AI37116"],"award-info":[{"award-number":["R01AI37116"]}],"id":[{"id":"10.13039\/100000060","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100006108","name":"National Center for Advancing Translational Sciences","doi-asserted-by":"publisher","award":["UL1TR002529"],"award-info":[{"award-number":["UL1TR002529"]}],"id":[{"id":"10.13039\/100006108","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100008113","name":"Indiana University-Purdue University Indianapolis","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100008113","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["journals.asm.org"],"crossmark-restriction":true},"short-container-title":["Infect Immun"],"published-print":{"date-parts":[[2025,5,13]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:sec>\n            <jats:title\/>\n            <jats:p>\n              <jats:italic toggle=\"yes\">Haemophilus ducreyi<\/jats:italic>\n              causes cutaneous ulcers in children who live in yaws-endemic countries and the genital ulcer disease chancroid. In the human host,\n              <jats:italic toggle=\"yes\">H. ducreyi<\/jats:italic>\n              resides in an abscess and may need to resist both heat and oxidative stress, which result in aggregation and misfolding of bacterial proteins. In\n              <jats:italic toggle=\"yes\">Escherichia coli<\/jats:italic>\n              , the\n              <jats:italic toggle=\"yes\">hslUV<\/jats:italic>\n              (\n              <jats:italic toggle=\"yes\">clpYQ<\/jats:italic>\n              ) operon encodes a proteasome-like complex that degrades misfolded proteins and is upregulated during heat shock. In previous studies, we showed that\n              <jats:italic toggle=\"yes\">hslUV<\/jats:italic>\n              transcripts are upregulated in experimental lesions caused by\n              <jats:italic toggle=\"yes\">H. ducreyi<\/jats:italic>\n              in human volunteers, suggesting that HslUV may help\n              <jats:italic toggle=\"yes\">H. ducreyi<\/jats:italic>\n              adapt to the abscess environment. Here, we constructed an unmarked\n              <jats:italic toggle=\"yes\">hslUV<\/jats:italic>\n              operon deletion mutant, 35000HP\u0394\n              <jats:italic toggle=\"yes\">hslUV<\/jats:italic>\n              , in\n              <jats:italic toggle=\"yes\">H. ducreyi<\/jats:italic>\n              . Whole-genome sequencing showed that compared to its parent (35000HP), the mutant contained only the deletion of interest. Six volunteers were inoculated at three sites on skin overlying the deltoid on opposite arms with 35000HP and 35000HP\u0394\n              <jats:italic toggle=\"yes\">hslUV<\/jats:italic>\n              . Within 24 h, papules formed at 88.9% (95% CI [69%, 100%]) at both parent and mutant-inoculated sites (\n              <jats:italic toggle=\"yes\">P<\/jats:italic>\n              = 1.0). Pustules formed at 44.4% (95% CI [25.6%, 64.3%]) at parent-inoculated sites and 33.3% (95% CI [2.5%, 64.1%]) at mutant-inoculated sites (\n              <jats:italic toggle=\"yes\">P<\/jats:italic>\n              = 0.17). Thus, the proteosome-like complex encoded by\n              <jats:italic toggle=\"yes\">hslUV<\/jats:italic>\n              was dispensable for\n              <jats:italic toggle=\"yes\">H. ducreyi<\/jats:italic>\n              virulence in humans. In the absence of\n              <jats:italic toggle=\"yes\">hslUV<\/jats:italic>\n              ,\n              <jats:italic toggle=\"yes\">H. ducreyi<\/jats:italic>\n              likely utilizes other systems such as the Lon protease, ClpXP, and ClpB\/DnaK to combat protein aggregation and misfolding, underscoring the importance of the functional redundancy of such systems in gram-negative pathogens.\n            <\/jats:p>\n          <\/jats:sec>","DOI":"10.1128\/iai.00577-24","type":"journal-article","created":{"date-parts":[[2025,4,10]],"date-time":"2025-04-10T13:57:11Z","timestamp":1744293431000},"update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":0,"title":["The protein degradation system encoded by\n            <i>hslUV<\/i>\n            (\n            <i>ClpYQ<\/i>\n            ) is dispensable for the virulence of\n            <i>Haemophilus ducreyi<\/i>\n            in human volunteers"],"prefix":"10.1128","volume":"93","author":[{"given":"Kate R.","family":"Fortney","sequence":"first","affiliation":[{"name":"Department of Microbiology and Immunology, Indiana University School of Medicine, Indiana University","place":["Indianapolis, USA"]}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-5277-3692","authenticated-orcid":true,"given":"Julie A.","family":"Brothwell","sequence":"additional","affiliation":[{"name":"Department of Microbiology and Immunology, Indiana University School of Medicine, Indiana University","place":["Indianapolis, USA"]}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Teresa A.","family":"Batteiger","sequence":"additional","affiliation":[{"name":"Department of Medicine, Indiana University School of Medicine, Indiana University","place":["Indianapolis, 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