Glycosylation of H4 influenza strains with pandemic potential and susceptibilities to lung surfactant SP-D

• DOI: 10.3389/fmolb.2023.1207670
• Publication Date: 2023-06-13T08:30:49Z
• Authors: Lisa M. Parsons; Olga Zoueva; Gabrielle Grubbs; Ewan Plant; Ewa Jankowska; Yijia Xie; Hao Song; George F. Gao; Zhiping Ye; Surender Khurana; John F. Cipollo
• Keywords: Surfactant protein D; Glycomics; Collectin

We recently reported that members of group 1 influenza A virus (IAV) containing H2, H5, H6, and H11 hemagglutinins (HAs) are resistant to lung surfactant protein D (SP-D). H3 viruses, 2 IAV, have high affinity for SP-D, which depends on the presence high-mannose glycans at glycosite N165 head HA. The low SP-D viruses is due complex an analogous HA, replacement with glycan this site evoked strong interaction SP-D. Thus, if IAV were make zoonotic leap humans, pathogenicity such strains could be problematic since as a first-line innate immunity factor in respiratory tissues, ineffective demonstrated vitro. Here, we extend these studies H4 representative those specificity avian or swine sialyl receptors, i.e., receptor-binding sites either Q226 G228 recent Q226L G228S mutations facilitate receptor specificity. latter increased potential humans switch from sialylα2,3 sialylα2,6 preference. better understanding action against will provide important information regarding pandemic risk strains. Our glycomics vitro analyses four HAs reveal SP-D-favorable glycosylation patterns. Therefore, susceptibilities defense align HA glycosylation.