{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,8]],"date-time":"2026-03-08T00:34:26Z","timestamp":1772930066738,"version":"3.50.1"},"reference-count":45,"publisher":"Oxford University Press (OUP)","issue":"4","license":[{"start":{"date-parts":[[2001,4,1]],"date-time":"2001-04-01T00:00:00Z","timestamp":986083200000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/academic.oup.com\/pages\/standard-publication-reuse-rights"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2001,4,1]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>Pneumocystis carinii continues to cause severe pneumonia in immunocompromised patients. Surfactant protein D (SP-D), a lung collectin, markedly accumulates during P. carinii pneumonia and binds to glycoprotein A (gpA) on the surface of P. carinii, thereby enhancing interactions with alveolar macrophages. Herein, we report the structural basis of the interaction of SP-D with gpA. We demonstrate that natural SP-D binds to purified gpA in the presence of 2 mM calcium in a saturable, concentration-dependent manner, which is abolished by 10 mM ethylenediaminetetraacetic acid. Increasing concentrations of calcium under otherwise cation-free conditions significantly enhance SP-D binding to gpA, whereas manganese and magnesium cations have minimal effect. Maximal SP-D binding occurs at pH 7.4, with significant inhibition at pH 4. SP-D binding to gpA is also competitively inhibited by maltose &amp;gt; glucose &amp;gt; mannose &amp;gt; N-acetyl-glucosamine. Comparison of the binding of various natural and recombinant forms of SP-D to gpA reveals that the number of carbohydrate recognition domains (CRDs) in a given SP-D form determines the relative extent of binding to gpA. Maximal binding is observed with natural SP-D (dodecamers and higher order SP-D complexes) followed by recombinant dodecamers. In contrast, recombinant full-length trimers exhibit substantially less binding, which is similar to that observed with a recombinant truncated molecule consisting of the CRD and neck regions, and containing trimers of this portion of the molecule. Taken together, these findings strongly indicate that the CRD of SP-D mediates interaction with P. carinii gpA through its attached oligosaccharides and that the extent of SP-D binding to P. carinii is greatest with dodecamers and higher order forms of SP-D.<\/jats:p>","DOI":"10.1165\/ajrcmb.24.4.3504","type":"journal-article","created":{"date-parts":[[2013,4,3]],"date-time":"2013-04-03T21:23:21Z","timestamp":1365024201000},"page":"475-484","source":"Crossref","is-referenced-by-count":45,"title":["Carbohydrate Recognition Domain of Surfactant Protein D Mediates Interactions with\n                    <i>Pneumocystis carinii<\/i>\n                    Glycoprotein A"],"prefix":"10.1093","volume":"24","author":[{"given":"Zvezdana","family":"Vuk-Pavlovic","sequence":"first","affiliation":[{"name":"Thoracic Diseases Research Unit, Division of Pulmonary, Critical Care, and Internal Medicine, and Department of Biochemistry and Molecular Biology, Mayo Clinic and Foundation, Rochester, Minnesota; and Department of Pathology, Jewish Hospital at Washington University, St. Louis, Missouri"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Joseph E.","family":"Standing","sequence":"additional","affiliation":[{"name":"Thoracic Diseases Research Unit, Division of Pulmonary, Critical Care, and Internal Medicine, and Department of Biochemistry and Molecular Biology, Mayo Clinic and Foundation, Rochester, Minnesota; and Department of Pathology, Jewish Hospital at Washington University, St. Louis, Missouri"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Erika C.","family":"Crouch","sequence":"additional","affiliation":[{"name":"Thoracic Diseases Research Unit, Division of Pulmonary, Critical Care, and Internal Medicine, and Department of Biochemistry and Molecular Biology, Mayo Clinic and Foundation, Rochester, Minnesota; and Department of Pathology, Jewish Hospital at Washington University, St. Louis, Missouri"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Andrew H.","family":"Limper","sequence":"additional","affiliation":[{"name":"Thoracic Diseases Research Unit, Division of Pulmonary, Critical Care, and Internal Medicine, and Department of Biochemistry and Molecular Biology, Mayo Clinic and Foundation, Rochester, Minnesota; and Department of Pathology, Jewish Hospital at Washington University, St. Louis, Missouri"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"286","published-online":{"date-parts":[[2001,4,1]]},"reference":[{"key":"2026030700034200200_B1","doi-asserted-by":"crossref","first-page":"519","DOI":"10.1038\/334519a0","article-title":"Ribosomal RNA sequences show Pneumocystis carinii to be a member of the fungi.","volume":"334","author":"Edman","year":"1988","journal-title":"Nature"},{"key":"2026030700034200200_B2","doi-asserted-by":"crossref","first-page":"5","DOI":"10.4065\/71.1.5","article-title":"Pneumocystis carinii pneumonia in patients without acquired immunodeficiency syndrome: associated disorders and prior corticosteroid therapy.","volume":"71","author":"Yale","year":"1996","journal-title":"Mayo Clin. 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