Unusual molecular architecture of the machupo virus attachment glycoprotein.
نویسندگان
چکیده
New World arenaviruses, which cause severe hemorrhagic fever, rely upon their envelope glycoproteins for attachment and fusion into their host cell. Here we present the crystal structure of the Machupo virus GP1 attachment glycoprotein, which is responsible for high-affinity binding at the cell surface to the transferrin receptor. This first structure of an arenavirus glycoprotein shows that GP1 consists of a novel alpha/beta fold. This provides a blueprint of the New World arenavirus attachment glycoproteins and reveals a new architecture of viral attachment, using a protein fold of unknown origins.
منابع مشابه
Machupo Virus Glycoprotein Determinants for Human Transferrin Receptor 1 Binding and Cell Entry
Machupo virus (MACV) is a highly pathogenic New World arenavirus that causes hemorrhagic fever in humans. MACV, as well as other pathogenic New World arenaviruses, enter cells after their GP1 attachment glycoprotein binds to their cellular receptor, transferrin receptor 1 (TfR1). TfR1 residues essential for this interaction have been described, and a co-crystal of MACV GP1 bound to TfR1 suggest...
متن کاملMolecular Farming, an Effective System for the Production of Immunogenic Crimean-Congo Hemorrhagic Fever Virus Glycoprotein
The main aim of this study was to obtain the Crimean-Congo hemorrhagic fever virus (CCHFV) glycoprotein, through either stable transgenic plants or using a transient expression system, and determine the yield, quality and finally the immunogenicity of the plant-made CCHFV glycoprotein in a mouse model. We designed and synthesized a codon-optimized G1/G2 gene from the G1 and G2 parts of the CCHF...
متن کاملA Sensitive Neutralization Assay for Influenza C Viruses Based on the Acetylesterase Activity HEF Glycoprotein
Influenza C virus possesses specific neuraminate-O-acetylesterase as a receptor-destroying function. This enzymatic activity of the viral glycoprotein HEF (Hemagglutinin, esterase activity and fusion factor) can be visualized in situ by the use of distinct color substrates. Hereby the localization, as well as the quantity of synthesized HEF protein is detectable. We further developed the estera...
متن کاملIdentification of Aptamer-Binding Sites in Hepatitis C Virus Envelope Glycoprotein E2
Hepatitis C Virus (HCV) encodes two envelope glycoproteins, E1 and E2. Our previous work selected a specific aptamer ZE2, which could bind to E2 with high affinity, with a great potential for developing new molecular probes as an early diagnostic reagents or therapeutic drugs targeting HCV. In this study, the binding sites between E2 and aptamer ZE2 were further explored. E2 was truncated to 15...
متن کاملAnalyzing machupo virus-receptor binding by molecular dynamics simulations
In many biological applications, we would like to be able to computationally predict mutational effects on affinity in protein-protein interactions. However, many commonly used methods to predict these effects perform poorly in important test cases. In particular, the effects of multiple mutations, non alanine substitutions, and flexible loops are difficult to predict with available tools and p...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
عنوان ژورنال:
- Journal of virology
دوره 83 16 شماره
صفحات -
تاریخ انتشار 2009