NMR Experiments Reveal the Molecular Basis of Receptor Recognition by a Calicivirus

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• 作者：Christoph Rademacher ; N. Rama Krishna ; Monica Palcic ; Francisco Parra ; Thomas Peters
• 刊名：Journal of the American Chemical Society
• 出版年：2008
• 出版时间：March 19, 2008
• 年：2008
• 卷：130
• 期：11
• 页码：3669 - 3675
• 全文大小：255K
• 年卷期：v.130,no.11(March 19, 2008)
• ISSN：1520-5126

文摘

The analysis of virus-receptor interactions at atomic resolution is of fundamental importance tounderstand infection processes, and to establish novel anti-viral therapies. As an example, rabbithemorrhagic disease virus (RHDV), a member of the Caliciviridae family and considered as an "emerging"virus, attaches to histo-blood group antigens (HBGA) on the surface of adult rabbit epithelial cells of theupper respiratory and digestive tracts. It appears that this attachment is a key step in the process of infectionwith RHDV. Here, we report NMR experiments that reveal the atomic details of the recognition of HBGAsand fragments thereof by RHDV virus-like particles (VLP). The experiments yield binding epitopes of severalHBGAs and show that L-fucose is a minimal structural requirement for specific molecular recognition bythe VLPs. As the methodology is general, these studies may pave the way for the development of novelanti-viral entry inhibitors.