FIG 3.

Glycosylation on the head of HA modulates the efficiency of langerin-mediated infection of Lec2-Lg cells. (A) BJx109 infects Lec2-Lg cells efficiently, but the poorly glycosylated PR8 strain does not. Cells were infected with 10⁷ PFU of BJx109 or PR8, and the percentages of infected cells were determined using immunofluorescence at 6 to 8 h postinfection. (B) Glycosylation of the IAV HA modulates the ability of IAV to infect Lec2-Lg cells. Cells were infected with 10⁷ PFU of RG-PR8-Beij/89 HA/NA, RG-PR8, RG-PR8-Beij/89 HA, and RG-PR8-Beij/89 NA (panel i), or RG-PR8-Beij/89 HA, RG-PR8, and RG-PR8-Beij/89 HA + 94/131 (panel ii), and the percentages of infected cells were determined 6 to 8 h postinfection. (C) Lec2-ctrl or Lec2-Lg cell monolayers were infected with 5 × 10⁶ PFU of H3N2 strains Mem/71, Beij/89, and NY/04 or with H1N1 strains PR8, Braz/78, and Cal/09, and the percentages of infected cells were determined 6 to 8 h postinfection. Numbers in parentheses at the bottom of the panel indicate the number of potential N-linked glycosylation sites present on the head of the viral HA. For panels B and C, data represent the mean percent infection (±1 SD) and are representative of at least two independent experiments. Statistical significance was assessed using one-way ANOVA with Tukey's post hoc analysis (*, P < 0.05; **, P < 0.01; ***, P < 0.001.; n.s., not significant).