N-Linked Glycosylation Facilitates Sialic Acid-Independent Attachment and Entry of Influenza A Viruses into Cells Expressing DC-SIGN or L-SIGN

• DOI: 10.1128/jvi.01705-10
• Publication Date: 2010-12-30T01:48:28Z
• Authors: Sarah L. Londrigan; Stuart G. Turville; Michelle D. Tate; Yi-Mo Deng; Andrew G. Brooks; Patrick C. Reading
• Keywords: DC-SIGN

ABSTRACT It is widely recognized that sialic acid (SA) can mediate attachment of influenza virus to the cell surface, and yet specific receptors entry are not known. For many viruses, a definitive demonstration receptor function has been achieved when nonpermissive cells rendered susceptible infection following transfection gene encoding putative receptor. virus, such approaches have confounded by abundance SA on mammalian so it difficult identify lines infection. We examined Lec2 Chinese hamster ovary (CHO) cells, mutant line deficient in SA. CHO were resistant infection, stable expressing either DC-SIGN or L-SIGN generated assess potential each molecule as SA-independent for A viruses. Virus strain BJx109 (H3N2) bound Ca 2+ -dependent manner, transfected Treatment Lec2-DC-SIGN Lec2-L-SIGN with mannan, but bacterial neuraminidase, blocked finding consistent entry. Moreover, PR8 (H1N1) bears low levels mannose-rich glycans was inefficient at infecting L-SIGN, whereas other glycosylated H1N1 subtype viruses could infect efficiently. Together, these data indicate human C-type lectins (DC-SIGN L-SIGN) independently surface