{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,18]],"date-time":"2026-09-18T00:55:28Z","timestamp":1789692928518,"version":"4.0.1"},"reference-count":38,"publisher":"American Society for Microbiology","issue":"3","license":[{"start":{"date-parts":[[2001,3,1]],"date-time":"2001-03-01T00:00:00Z","timestamp":983404800000},"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":[[2001,3]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>\n            Cyanovirin-N (CV-N), an 11-kDa protein originally isolated from the cyanobacterium\n            <jats:italic>Nostoc ellipsosporum<\/jats:italic>\n            , potently inactivates diverse strains of human immunodeficiency virus type 1 (HIV-1), HIV-2, simian immunodeficiency virus, and feline immunodeficiency virus. It has been well established that the HIV surface envelope glycoprotein gp120 is a molecular target of CV-N. We recently reported that CV-N impaired the binding of virion-associated gp120 to cell-associated CD4 and that CV-N preferentially inhibited binding of the glycosylation-dependent neutralizing monoclonal antibody 2G12 to gp120. However, CV-N did not interfere with the interactions of soluble CD4 (sCD4) with either soluble gp120 (sgp120) or virion-associated gp120. In the present study, we have evaluated the effects of CV-N on the binding of sgp120 to cell-associated CD4 to clarify the experimental basis of the previous binding results, and we further address the detailed mechanism of action of CV-N. Here we present evidence that (i) CV-N impairs both CD4-dependent and CD4-independent binding of sgp120 to the target cells, (ii) CV-N blocks the sCD4-induced binding of sgp120 with cell-associated coreceptor CXCR4, and (iii) CV-N dissociates bound sgp120 from target cells. The results illustrate that the measured effects of CV-N on gp120-CD4 binding interactions depend upon the type of CD4 (soluble or cell associated), but not upon the type of gp120 (soluble or virion associated), employed in the experimental protocol. In addition, this study reinforces that CV-N acts uniquely to prevent essential interactions between the envelope glycoprotein and target cell receptors and further supports the potential broad utility of CV-N as a microbicide to prevent the transmission of HIV and AIDS.\n          <\/jats:p>","DOI":"10.1128\/aac.45.3.664-672.2001","type":"journal-article","created":{"date-parts":[[2002,7,27]],"date-time":"2002-07-27T10:06:42Z","timestamp":1027764402000},"page":"664-672","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":83,"title":["Cyanovirin-N, a Potent Human Immunodeficiency Virus-Inactivating Protein, Blocks both CD4-Dependent and CD4-Independent Binding of Soluble gp120 (sgp120) to Target Cells, Inhibits sCD4-Induced Binding of sgp120 to Cell-Associated CXCR4, and Dissociates Bound sgp120 from Target Cells"],"prefix":"10.1128","volume":"45","author":[{"given":"Toshiyuki","family":"Mori","sequence":"first","affiliation":[{"name":"<!--label omitted: 1-->Laboratory of Natural Products, Division of Basic Sciences, National Cancer Institute-Frederick, Cancer Research and Development Center, Frederick, Maryland 21702"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Michael R.","family":"Boyd","sequence":"additional","affiliation":[{"name":"<!--label omitted: 1-->Laboratory of Natural Products, Division of Basic Sciences, National Cancer Institute-Frederick, Cancer Research and Development Center, Frederick, Maryland 21702"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"235","reference":[{"key":"e_1_3_2_2_2","doi-asserted-by":"publisher","DOI":"10.1016\/0092-8674(89)90922-7"},{"key":"e_1_3_2_3_2","doi-asserted-by":"crossref","first-page":"14611","DOI":"10.1016\/S0021-9258(18)98730-2","article-title":"Structural characterization of a cross-reactive idiotype shared by monoclonal antibodies specific for the human CD4 molecule.","volume":"266","author":"Attanasio R.","year":"1991","unstructured":"Attanasio R. Dilley D. Buck D. Maino V. C. Lohman K. L. Kanda P. Kennedy R. C. Structural characterization of a cross-reactive idiotype shared by monoclonal antibodies specific for the human CD4 molecule. J. Biol. Chem. 266 1991 14611 14619","journal-title":"J. Biol. Chem."},{"key":"e_1_3_2_4_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.89.19.9339"},{"key":"e_1_3_2_5_2","first-page":"151","article-title":"HIV entry and tropism. When one receptor is not enough.","volume":"542","author":"Berger E. A.","year":"1998","unstructured":"Berger E. A. HIV entry and tropism. When one receptor is not enough. Adv. Exp. Med. Biol. 542 1998 151 157","journal-title":"Adv. Exp. Med. 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R.","year":"1997","unstructured":"Gustafson K. R. Sowder R. C. II Henderson L. E. Cardellina J. H. II McMahon J. B. Rajamani U. Pannell L. K. Boyd M. R. Isolation, primary sequence determination, and disulfide bond structure of cyanovirin-N, an anti-HIV (human immunodeficiency virus) protein from the cyanobacterium Nostoc ellipsosporum. Biochem. Biophys. Res. Commun. 238 1997 223 228","journal-title":"Biochem. Biophys. Res. 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