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Lung surfactant protein D (SP-D), a key factor in first-line innate immunity defense, removes influenza type A virus (IAV) through interaction with hemagglutinin (HA) head region high-mannose glycan(s). While it is known that both H1 and H3 HAs have one or more key high-mannose glycosites in the head region, little is known about similar glycosylation of LPAIV strains H2N1, H5N1, H6N1, or H11N9, which may pose future health risks. Here, we demonstrate that the hemagglutinins of LPAIV strains do not have the required high-mannose glycans and do not interact with SP-D, and that sequence analysis can predict glycan subtype, thus predicting the presence or absence of this virulence marker.<\/jats:p>","DOI":"10.1128\/jvi.01951-19","type":"journal-article","created":{"date-parts":[[2019,12,6]],"date-time":"2019-12-06T13:54:19Z","timestamp":1575640459000},"update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":13,"title":["Influenza Virus Hemagglutinins H2, H5, H6, and H11 Are Not Targets of Pulmonary Surfactant Protein D:\n            <i>N<\/i>\n            -Glycan Subtypes in Host-Pathogen Interactions"],"prefix":"10.1128","volume":"94","author":[{"given":"Lisa M.","family":"Parsons","sequence":"first","affiliation":[{"name":"Food and Drug Administration, Center for Biologics Evaluation and Research, Division of Bacterial, Parasitic and Allergenic 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