3P54

Crystal Structure of the Japanese Encephalitis Virus Envelope Protein, strain SA-14-14-2.

Summary for 3P54

• Entry DOI: 10.2210/pdb3p54/pdb
• Related: 1oke 1svb 1tg8 1uzg 2ala 2hg0 2i69
• Descriptor: envelope glycoprotein (2 entities in total)
• Functional Keywords: viral envelope proteins, structural genomics, fusion peptide, antibody epitopes, flavivirus, japanese encephalitis virus, center for structural genomics of infectious diseases, csgid, viral protein
• Biological source: Japanese encephalitis virus
• Cellular location: Envelope protein E: Virion membrane; Multi- pass membrane protein: Q99DQ9
• Total number of polymer chains: 1
• Total formula weight: 43686.28

Authors

Luca, V.C.,Nelson, C.A.,AbiMansour, J.P.,Diamond, M.S.,Fremont, D.H.,Center for Structural Genomics of Infectious Diseases (CSGID) (deposition date: 2010-10-07, release date: 2010-12-08, Last modification date: 2024-10-30)

Primary citation

Luca, V.C.,Abimansour, J.,Nelson, C.A.,Fremont, D.H.
Crystal structure of the Japanese encephalitis virus envelope protein.
J.Virol., 86:2337-2346, 2012

PubMed Abstract: Japanese encephalitis virus (JEV) is the leading global cause of viral encephalitis. The JEV envelope protein (E) facilitates cellular attachment and membrane fusion and is the primary target of neutralizing antibodies. We have determined the 2.1-Å resolution crystal structure of the JEV E ectodomain refolded from bacterial inclusion bodies. The E protein possesses the three domains characteristic of flavivirus envelopes and epitope mapping of neutralizing antibodies onto the structure reveals determinants that correspond to the domain I lateral ridge, fusion loop, domain III lateral ridge, and domain I-II hinge. While monomeric in solution, JEV E assembles as an antiparallel dimer in the crystal lattice organized in a highly similar fashion as seen in cryo-electron microscopy models of mature flavivirus virions. The dimer interface, however, is remarkably small and lacks many of the domain II contacts observed in other flavivirus E homodimers. In addition, uniquely conserved histidines within the JEV serocomplex suggest that pH-mediated structural transitions may be aided by lateral interactions outside the dimer interface in the icosahedral virion. Our results suggest that variation in dimer structure and stability may significantly influence the assembly, receptor interaction, and uncoating of virions.

PubMed: 22156523
DOI: 10.1128/JVI.06072-11

Experimental method

X-RAY DIFFRACTION (2.097 Å)