5T9Y

Crystal structure of the infectious salmon anemia virus (ISAV) hemagglutinin-esterase protein

Summary for 5T9Y

• Entry DOI: 10.2210/pdb5t9y/pdb
• Related: 5T96
• Descriptor: HE protein, MAGNESIUM ION, GLYCEROL, ... (6 entities in total)
• Functional Keywords: 4-0-acetylsialic acid, hydrolase, hemagglutinin, coiled-coil, viral receptor-complex, infectious salmon anemia virus, isav, viral protein
• Biological source: Infectious salmon anemia virus
• Total number of polymer chains: 3
• Total formula weight: 115523.33

Authors

Cook, J.D.,Sultana, A.,Lee, J.E. (deposition date: 2016-09-09, release date: 2017-03-22, Last modification date: 2024-11-06)

Primary citation

Cook, J.D.,Sultana, A.,Lee, J.E.
Structure of the infectious salmon anemia virus receptor complex illustrates a unique binding strategy for attachment.
Proc. Natl. Acad. Sci. U.S.A., 114:E2929-E2936, 2017

PubMed Abstract: Orthomyxoviruses are an important family of RNA viruses, which include the various influenza viruses. Despite global efforts to eradicate orthomyxoviral pathogens, these infections remain pervasive. One such orthomyxovirus, infectious salmon anemia virus (ISAV), spreads easily throughout farmed and wild salmonids, constituting a significant economic burden. ISAV entry requires the interplay of the virion-attached hemagglutinin-esterase and fusion glycoproteins. Preventing infections will rely on improved understanding of ISAV entry. Here, we present the crystal structures of ISAV hemagglutinin-esterase unbound and complexed with receptor. Several distinctive features observed in ISAV HE are not seen in any other viral glycoprotein. The structures reveal a unique mode of receptor binding that is dependent on the oligomeric assembly of hemagglutinin-esterase. Importantly, ISAV hemagglutinin-esterase receptor engagement does not initiate conformational rearrangements, suggesting a distinct viral entry mechanism. This work improves our understanding of ISAV pathogenesis and expands our knowledge on the overall diversity of viral glycoprotein-mediated entry mechanisms. Finally, it provides an atomic-resolution model of the primary neutralizing antigen critical for vaccine development.

PubMed: 28320973
DOI: 10.1073/pnas.1617993114

Experimental method

X-RAY DIFFRACTION (1.8 Å)