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1.
Fig 7

Fig 7. From: Adaptation of a Duck Influenza A Virus in Quail.

Infection of human respiratory tissue by influenza A viruses adapted in quail. Bronchus was incubated with the P19T virus (a), the parent A/duck/Mongolia/301/01 virus (b), A/duck/Vietnam/5001/04 (H5N1) virus (e), or human A/Kawasaki/173/01(H1N1) virus (f). Alveoli were incubated with the P19T virus (c) or the parent A/duck/Mongolia/301/01 virus (d), A/duck/Vietnam/5001/04 virus (g), or A/Kawasaki/173/01(H1N1) virus (h). Virus-infected cells are stained brown. Note that the P19T and human-derived viruses could infect the bronchial epithelium.

Shinya Yamada, et al. J Virol. 2012 February;86(3):1411-1420.
2.
Fig 2

Fig 2. From: Adaptation of a Duck Influenza A Virus in Quail.

Growth of a duck influenza virus (H3N2) in different quail organs during passages. Virus was serially passaged in quail (three quail per passage) 19 times with 0.5 ml of 10% pooled organ homogenate of nasal turbinate, trachea, lung, and colon every 3 days. The indicated organs from three animals were pooled in each passage, and virus in the organs was titrated to determine the TCID50 by using MDCK cells.

Shinya Yamada, et al. J Virol. 2012 February;86(3):1411-1420.
3.
Fig 3

Fig 3. From: Adaptation of a Duck Influenza A Virus in Quail.

Locations of HA and NA mutations. (A) Three-dimensional structure of the HA trimer (3) showing the locations of the mutations found in the P19T virus. (B) Structure of the receptor binding site (130 loop [brown], 220 loop [blue], and 190 helix [green]) of the HA molecule. The mutations discussed in the text are indicated. (C) Three-dimensional structure of the NA monomer (41) showing the locations of the mutations found in the P19T virus. The structure of the stalk is not solved; the line shown to indicate the stalk is for illustration purposes.

Shinya Yamada, et al. J Virol. 2012 February;86(3):1411-1420.
4.
Fig 6

Fig 6. From: Adaptation of a Duck Influenza A Virus in Quail.

Virus growth kinetics in different animal cells. (a to c) Comparison of growth among the WT(HA,NA)-RG, P19Tcl2(HA,NA)-RG, and P19Tcl4(HA,NA)-RG viruses in DEF (a), CEF(b), and MDCK cells (c). (d) Comparison of growth among the WT(HA,NA)-human-RG, P19Tcl2(HA,NA)-human-RG, and P19Tcl4(HA,NA)-human-RG viruses in NHBE cells. DEF, CEF, and MDCK and NHBE cells were infected with virus at an MOI of 0.001 PFU/cell. At the indicated times postinfection, the virus was titrated using MDCK cells. The results are presented as means ± standard deviations of triplicate experiments.

Shinya Yamada, et al. J Virol. 2012 February;86(3):1411-1420.
5.
Fig 5

Fig 5. From: Adaptation of a Duck Influenza A Virus in Quail.

Comparison of virus release from erythrocytes. Viruses (128 HA units as measured by using chicken or guinea pig erythrocytes) were incubated with chicken (a) or guinea pig (b) RBCs at 4°C and then incubated at 37°C. At the indicated time points, HA titers were determined. (a) The efficiency with which virus was eluted from chicken RBCs was almost the same for WT(HA,NA)-RG, WT(HA)-P19Tcl2(NA)-RG, and WT(HA)-P19Tcl4(NA)-RG. (b) However, WT(HA)-P19Tcl2(NA)-RG and WT(HA)-P19Tcl4(NA)-RG were released from guinea pig RBCs at a lower efficiency than WT(HA,NA)-RG. The data presented are representative of three independent experiments.

Shinya Yamada, et al. J Virol. 2012 February;86(3):1411-1420.
6.
Fig 1

Fig 1. From: Adaptation of a Duck Influenza A Virus in Quail.

Reactivity of quail organs with sialic acid linkage-specific lectins. At middle right, the anatomy of the airway of the quail is shown schematically, indicating the tissues used for panels A thru E. (A) Respiratory region of the nasal turbinate. Siaα2-6Gal is prominent on the mucosal surface (green, fluorescein-labeled S. nigra lectin). (B) Olfactory region of the nasal turbinate. Siaα2-6Gal is prominent on the surface of the mucosal epithelium (green). Although the secretory substances contained Siaα2-6Gal (arrows), some of the secretory cells expressed both Siaα2-3Gal and Siaα2-6Gal (yellow, overlapping orange-red staining with Alexa Fluor 594-labeled M. amurensis lectin II; arrowheads). (C) Trachea. The mucosal epithelium predominantly contains Siaα2-6Gal. Some of the secretory material in the goblet cells contains predominantly Siaα2-3Gal (red; arrows), whereas some contains both Siaα2-3Gal and Siaα2-6Gal (yellow; arrowheads). (D) Mesobronchus. The predominance of the Siaα2-6Gal linkage on the mucosal surface is apparent. (E) Parabronchus. Either S. nigra lectin or M. amurensis lectin II binding was detected in the epithelial cells of the parabronchus. The border between the cell surface and the ductal lumen is indicated with dashed lines in the inset. SM, smooth muscle; CT, connective tissue. The inset images correspond to the dashed squares of the main figure. (F) Colon. Both Siaα2-3Gal and Siaα2-6Gal are abundant in the lower crypt (yellow), although Siaα2-6Gal is predominant in the epithelium of the upper crypt. (G) Diagram for histological orientation. L, lumen of the colon; C, crypt of the colon. (H) Duck colon. Siaα2-3Gal can be seen throughout the mucosal surface (red; white arrows). (I) Diagram for histological orientation. L, lumen of the colon; C, crypt of the colon. The asterisks indicate the luminal side of the ducts. DAPI was used for counterstaining.

Shinya Yamada, et al. J Virol. 2012 February;86(3):1411-1420.
7.
Fig 4

Fig 4. From: Adaptation of a Duck Influenza A Virus in Quail.

Receptor specificity of the parent and quail-passaged duck viruses. (A) The receptor assay relies on the inhibition of virus binding to fetuin [which possesses both α(2-3)- and α(2-6)-linked sialic acids] with sialylglycoconjugate polymers that possess either α(2-3)-linked (blue line) or α(2-6)-linked (red line) sialic acid. The binding activities of the parent duck virus (a), P19T virus (b), P19T clone 2 (c), and P19T clone 4 (d) were determined based on absorbance at 490 nm (minus the background level). A/duck/Vietnam/5001/04 (H5N1) (e) and A/Kawsaki/173/01(H1N1) (f) served as positive controls. Fetuin binding of the parent virus and the quail-passaged viruses was not inhibited by a polymer possessing α2-6-linked sialic acid. The data presented are representative of three independent experiments. (B) Glycan microarray assay. Purified whole virions were used for these assays. The microarrays displayed 86 sialylated glycans and 9 asialoglycans printed on coated glass slides. Different types of glycans on the array (x axis) are highlighted in different colors; the identity of each numbered glycan is provided in Table S1 in the supplemental material. The black bars denote the mean fluorescent binding signal intensities (y axis) of 4 spots; the standard errors are shown as red extensions. The data presented are representative of three independent experiments.

Shinya Yamada, et al. J Virol. 2012 February;86(3):1411-1420.

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