{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,6,4]],"date-time":"2026-06-04T16:28:07Z","timestamp":1780590487504,"version":"3.54.1"},"reference-count":45,"publisher":"American Society for Microbiology","issue":"12","license":[{"start":{"date-parts":[[2000,12,1]],"date-time":"2000-12-01T00:00:00Z","timestamp":975628800000},"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":["Antimicrob Agents Chemother"],"published-print":{"date-parts":[[2000,12]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>\n            Salivary histatins are a family of basic histidine-rich proteins in which therapeutic potential as drugs against oral candidiasis is apparent, considering their potent in vitro antifungal activity and lack of toxicity to humans. Histatin 5 (Hst 5) kills the fungal pathogen\n            <jats:italic>Candida albicans<\/jats:italic>\n            via a mechanism that involves binding to specific sites on the yeast cell membrane and subsequent release of cellular ATP in the absence of cytolysis. We explored the killing pathway activated by Hst 5 and compared it to those activated by other antifungal agents. The candidacidal activity of human neutrophil defensin 1 (HNP-1) shared very similar features to Hst 5 cytotoxic action with respect to active concentrations and magnitude of induction of nonlytic ATP efflux, depletion of intracellular ATP pools, and inhibitor profile. Hst 5 and HNP-1 are basic proteins of about 3 kDa; however, they have unique primary sequences and solution structures that cannot explain how these two molecules act so similarly on\n            <jats:italic>C. albicans<\/jats:italic>\n            to induce cell death. Our finding that HNP-1 prevented Hst 5 binding to the candidal Hst 5 binding protein suggests that the basis for the overlapping actions of these two naturally occurring antimicrobial proteins may involve interactions with shared yeast components.\n          <\/jats:p>","DOI":"10.1128\/aac.44.12.3310-3316.2000","type":"journal-article","created":{"date-parts":[[2002,7,27]],"date-time":"2002-07-27T10:06:42Z","timestamp":1027764402000},"page":"3310-3316","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":95,"title":["Salivary Histatin 5 and Human Neutrophil Defensin 1 Kill\n            <i>Candida albicans<\/i>\n            via Shared Pathways"],"prefix":"10.1128","volume":"44","author":[{"given":"Mira","family":"Edgerton","sequence":"first","affiliation":[{"name":"<!--label omitted: 1-->Departments of Oral Biology,1"},{"name":"<!--label omitted: 2-->Restorative Dentistry,2 and"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Svetlana E.","family":"Koshlukova","sequence":"additional","affiliation":[{"name":"<!--label omitted: 1-->Departments of Oral Biology,1"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Marcelo W. B.","family":"Araujo","sequence":"additional","affiliation":[{"name":"<!--label omitted: 1-->Departments of Oral Biology,1"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Rashmi C.","family":"Patel","sequence":"additional","affiliation":[{"name":"<!--label omitted: 1-->Departments of Oral Biology,1"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jin","family":"Dong","sequence":"additional","affiliation":[{"name":"<!--label omitted: 1-->Departments of Oral Biology,1"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jeremy A.","family":"Bruenn","sequence":"additional","affiliation":[{"name":"<!--label omitted: 3-->Biological Sciences,3 State University of New York at Buffalo, Buffalo, New York 14214"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"235","reference":[{"key":"e_1_3_2_2_2","doi-asserted-by":"publisher","DOI":"10.1093\/jac\/24.6.905"},{"key":"e_1_3_2_3_2","doi-asserted-by":"publisher","DOI":"10.1128\/AAC.26.1.22"},{"key":"e_1_3_2_4_2","doi-asserted-by":"publisher","DOI":"10.1128\/AAC.38.2.363"},{"key":"e_1_3_2_5_2","doi-asserted-by":"crossref","unstructured":"Bolard\n              J.\n          Mechanism of action of an anti- Candida drug: amphotericin B and its derivatives\n          Candida albicans: cellular and molecular biology.\n              Prasad\n              R.\n          1991\n          215\n          238\n          Springer-Verlag\n          Berlin Germany","DOI":"10.1007\/978-3-642-75253-7_14"},{"key":"e_1_3_2_6_2","doi-asserted-by":"publisher","DOI":"10.1177\/00220345950740050301"},{"key":"e_1_3_2_7_2","doi-asserted-by":"publisher","DOI":"10.1128\/AAC.40.2.419"},{"key":"e_1_3_2_8_2","first-page":"465","article-title":"Interactions of Candida albicans yeast cells, germ tubes and hyphae with human polymorphonuclear leukocytes in vitro.","volume":"130","author":"Cockayne A.","year":"1984","unstructured":"Cockayne A. 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