Avian Influenza Viruses Infect Primary Human Bronchial Epithelial Cells Unconstrained by Sialic Acid alpha 2,3 Residues

• Type of Material: Article
• Authors: Christine M. Oshansky, University of Georgia; Jennifer A. Pickens, University of Georgia; Konrad C. Bradley, Emory University; Les P. Jones, University of Georgia; Geraldine M. Saavedra-Ebner, University of Georgia; James P. Barber, University of Georgia; Jackelyn M. Crabtree, University of Georgia; David Steinhauer, Emory University; S. Mark Tompkins, University of Georgia; Ralph A. Tripp, University of Georgia
• Language: English
• Date: 2011-06-23
• Publisher: Public Library of Science
• Publication Version: Final Published Version
• Copyright Statement: © 2011 Oshansky et al.
• License: Creative Commons Attribution 4.0 International
• Final Published Version (URL): http://dx.doi.org/10.1371/journal.pone.0021183
• Title of Journal or Parent Work: PLoS ONE
• ISSN: 1932-6203
• Volume: 6
• Issue: 6
• Start Page: e21183
• End Page: e21183
• Grant/Funding Information: This work was funded by the Center of Excellence for Influenza Research and Surveillance (CEIRS) contract HHSN266200700006C and the Georgia Research Alliance (http://www.gra.org/).
• Keywords: HUMAN ALVEOLAR; CYTOKINE RESPONSES; Viral replication; Viral pathogens; Multidisciplinary Sciences; Influenza viruses; Sialic acids; HOST-RANGE; H5N1; GENE-EXPRESSION; RECEPTOR-BINDING SPECIFICITY; Influenza; MAACKIA-AMURENSIS; Influenza A virus; I INTERFERON RESPONSE; HUMAN AIRWAY EPITHELIUM; H1N1; Respiratory infections
• Research Categories: Biology, Virology; Biology, Microbiology; Health Sciences, Public Health

Abstract

Avian influenza viruses (AIV) are an important emerging threat to public health. It is thought that sialic acid (sia) receptors are barriers in cross-species transmission where the binding preferences of AIV and human influenza viruses are sias α2,3 versus α2,6, respectively. In this study, we show that a normal fully differentiated, primary human bronchial epithelial cell model is readily infected by low pathogenic H5N1, H5N2 and H5N3 AIV, which primarily bind to sia α2,3 moieties, and replicate in these cells independent of specific sias on the cell surface. NHBE cells treated with neuraminidase prior to infection are infected by AIV despite removal of sia α2,3 moieties. Following AIV infection, higher levels of IP-10 and RANTES are secreted compared to human influenza virus infection, indicating differential chemokine expression patterns, a feature that may contribute to differences in disease pathogenesis between avian and human influenza virus infections in humans.