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# Modis et al (2005) J Virology
- URL: https://www.hibiotech.com/press-modis-et-al-2005-j-virology/
- Published: 2005-01-01T12:00:00.000Z
- Updated: 2026-10-24T18:57:02.000Z
- Description: From the Hawaii Biotech archive: Journal of Virology: Volume 79, No.2, January 2005, Pages 1223-1231
- Author: The Hi, Biotech Newsroom
- Tags: Press Archive, Publication

Hi, Biotech is an independent publication with no affiliation with Hawaii Biotech, Inc. This page preserves a historical record from the company's original press archive, republished for research and archival purposes. Copyright in the original material remains with its original owner.

Variable Surface Epitopes in the Crystal Structure of Dengue Virus Type 3 Envelope Glycoprotein Yorgo Modis1, Steven Ogata2, David Clements2, and Stephen C. Harrison1

(1) Howard Hughes Medical Institute, Children's Hospital and Harvard Medical School, Boston, Massachusetts (2) Hawaii Biotech, Inc, 99-193 Aiea Heights Dr., Suite 200 Aiea, HI 96701, USA

Journal of Virology: Volume 79, No.2, January 2005, Pages 1223-1231

Abstract Dengue virus is an emerging global health threat. The major envelope glycoprotein, E, mediates viral attachment and entry by membrane fusion. Antibodies that bind but fail to neutralize noncognate serotypes enhance infection. We have determined the crystal structure of a soluble fragment of the envelope glycoprotein E from dengue virus type 3\. The structure closely resembles those of E proteins from dengue type 2 and tick-borne encephalitis viruses. Serotype-specific neutralization escape mutants in dengue virus E proteins are all located on a surface of domain III, which has been implicated in receptor binding. While antibodies against epitopes in domain I are nonneutralizing in dengue virus, there are neutralizing antibodies t hat recognize serotype-conserved epitopes in domain II. The mechanism of neutralization for these antibodies is probably inhibition of membrane fusion. Our structure shows that neighboring glycans on the viral surface are spaced widely enough (at least 32 Å) t hat they can interact with multiple carbohydrate recognition domains on oligomeric lectins such as DC-SIGN, ensuring maximum affinity for these putative receptors.

Link to full-text article: http://jvi.asm.org/cgi/content/full/79/2/1223?view=long&pmid=15613349