8VCC

Crystal structure of H19 influenza A virus hemagglutinin from A/lesser scaup/California/3087/2010

Summary for 8VCC

• Entry DOI: 10.2210/pdb8vcc/pdb
• Descriptor: hemagglutinin, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (4 entities in total)
• Functional Keywords: hemagglutinin, influenza a virus, h19, viral protein
• Biological source: Influenza A virus (A/lesser scaup/California/3087/2010)
• Total number of polymer chains: 1
• Total formula weight: 61574.37

Authors

Kottur, J.,Aggarwal, A.K. (deposition date: 2023-12-14, release date: 2024-07-03, Last modification date: 2024-10-30)

Primary citation

Karakus, U.,Mena, I.,Kottur, J.,El Zahed, S.S.,Seoane, R.,Yildiz, S.,Chen, L.,Plancarte, M.,Lindsay, L.,Halpin, R.,Stockwell, T.B.,Wentworth, D.E.,Boons, G.J.,Krammer, F.,Stertz, S.,Boyce, W.,de Vries, R.P.,Aggarwal, A.K.,Garcia-Sastre, A.
H19 influenza A virus exhibits species-specific MHC class II receptor usage.
Cell Host Microbe, 32:1089-1102.e10, 2024

PubMed Abstract: Avian influenza A virus (IAV) surveillance in Northern California, USA, revealed unique IAV hemagglutinin (HA) genome sequences in cloacal swabs from lesser scaups. We found two closely related HA sequences in the same duck species in 2010 and 2013. Phylogenetic analyses suggest that both sequences belong to the recently discovered H19 subtype, which thus far has remained uncharacterized. We demonstrate that H19 does not bind the canonical IAV receptor sialic acid (Sia). Instead, H19 binds to the major histocompatibility complex class II (MHC class II), which facilitates viral entry. Unlike the broad MHC class II specificity of H17 and H18 from bat IAV, H19 exhibits a species-specific MHC class II usage that suggests a limited host range and zoonotic potential. Using cell lines overexpressing MHC class II, we rescued recombinant H19 IAV. We solved the H19 crystal structure and identified residues within the putative Sia receptor binding site (RBS) that impede Sia-dependent entry.

PubMed: 38889725
DOI: 10.1016/j.chom.2024.05.018

Experimental method

X-RAY DIFFRACTION (2.383 Å)