Results: 4

1.
Figure 4

Figure 4. Glycan interactions within the NY107 RBS.. From: Structures of Receptor Complexes of a North American H7N2 Influenza Hemagglutinin with a Loop Deletion in the Receptor Binding Site.

The top panel shows the interactions of NY107 with (A) 3′SLN, (B) 6′SLN and (C) LSTb. NY107 is shown in orange/red/magenta cartoon respectively. The interacting HA residues are shown as green sticks. The bottom panel shows the electron density map of the ligands. The NY107 is shown in the same colors as above, and the ligands are shown as green sticks, the 2fo-fc electron density maps (contoured at 1σ) are shown in grey. Simulated annealing omit maps are shown in supplementary Figure S4.

Hua Yang, et al. PLoS Pathog. 2010 September;6(9):e1001081.
2.
Figure 3

Figure 3. Effect of 220-loop deletion and additional RBS mutations on NY107 receptor specificity.. From: Structures of Receptor Complexes of a North American H7N2 Influenza Hemagglutinin with a Loop Deletion in the Receptor Binding Site.

NY107 was engineered to restore the 220-loop to a consensus full-length HA from 1996 (A) and additional co-variant amino acid substitutions, Glu186Gly (B), Arg205Gly (C) and the double mutant Glu186Gly/Arg205Gly (D) to restore, on the NY107 framework, an HA RBS found in viruses prior to the introduction of the deletion in North American viruses. Colored bars group glycans as described in Figure 3. Error bars reflect the standard error in the signal for six independent replicates on the array. Structures of each of the numbered glycans are found in Table S4.

Hua Yang, et al. PLoS Pathog. 2010 September;6(9):e1001081.
3.
Figure 2

Figure 2. Receptor specificity of NY107 recHA and virus.. From: Structures of Receptor Complexes of a North American H7N2 Influenza Hemagglutinin with a Loop Deletion in the Receptor Binding Site.

Glycan microarray analysis of recombinant NY107 HA (A) and NY107 virus (B) compared to the recHA (C) and virus (D) from a Eurasian lineage A/Netherlands/219/2003 H7 influenza virus that was circulating in the same year and also infected a human. Colored bars highlight glycans that contain α2-3 SA (blue) and α2-6 SA (red), α2-6/α2-3 mixed SA (purple), N-glycolyl SA (green), α2-8 SA (brown), β2-6 and 9-O-acetyl SA, and non-SA (grey). Error bars reflect the standard error in the signal for six independent replicates on the array. Structures of each of the numbered glycans are found in Table S4.

Hua Yang, et al. PLoS Pathog. 2010 September;6(9):e1001081.
4.
Figure 1

Figure 1. NY107 HA monomer and comparison of its RBS to other HA structures.. From: Structures of Receptor Complexes of a North American H7N2 Influenza Hemagglutinin with a Loop Deletion in the Receptor Binding Site.

(A) One monomer is shown with the HA1 chain colored in green and the HA2 chain in cyan. The location of the receptor binding site and the HA1/HA2 cleavage site are circled. (B) The superposition of receptor binding domains of NY107 (green), Av-H7 (marine), 1918-Hu-H1 (magenta), Hu-H5 (yellow), Hu-H3 (orange), and Sw-H9 (grey). The proximity of Arg220 and Gln226 are highlighted. Three structural elements comprising this binding site are labeled. The two major differences are the extended 150-loop and the deletion of 220-loop of NY107. (C) Overlap of NY107 (green) and Av-H7 (marine) (PDB: 1TI8) illustrates the compensatory effect of R220 bringing it close to the position occupied by G228 in the avian HA. (D) Overlap of the NY107 (green), NY107- 3′SLN (orange), NY107-6′SLN (red), and NY107-LSTb (magenta) structures. All the figures were generated and rendered with the use of MacPyMOL [56].

Hua Yang, et al. PLoS Pathog. 2010 September;6(9):e1001081.

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