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Infection of swine ex vivo tissues with avian viruses including H7N9 and correlation with glycomic analysis.

Chan RW, Karamanska R, Van Poucke S, Van Reeth K, Chan IW, Chan MC, Dell A, Peiris JS, Haslam SM, Guan Y, Nicholls JM - Influenza Other Respir Viruses (2013)

Bottom Line: There was a greater abundance of Gal-α-Gal linkages resulting in a relative decrease in sialylated glycans.The swine respiratory tract also had a greater proportion of glycans containing Neu5Gc and Siaα2-6 glycans than the human respiratory tract.In contrast to previous studies we found that there was not as much expression of Siaα2-3 glycans on the surface of the trachea.

View Article: PubMed Central - PubMed

Affiliation: Department of Pathology, School of Public Health, Li Ka Shing Faculty of Medicine, The University of Hong Kong, Pokfulam, Hong Kong SAR, China; Centre of Influenza Research, School of Public Health, Li Ka Shing Faculty of Medicine, The University of Hong Kong, Pokfulam, Hong Kong SAR, China.

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N‐glycan profile of swine lung following sialidase treatment. Partial MALDI‐TOF MS profiles of the permethylated N‐linked glycans derived from swine trachea after digestion with sialidase S (α2‐3 specific) or sialidase A (α2‐3 and α2‐6 specific). Data were obtained from the 50% acetonitrile fraction and all molecular ions are present in sodiated form ([M+Na]+). Sialylated species are annotated in red and those with GalαGal are annotated in blue.
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irv12144-fig-0002: N‐glycan profile of swine lung following sialidase treatment. Partial MALDI‐TOF MS profiles of the permethylated N‐linked glycans derived from swine trachea after digestion with sialidase S (α2‐3 specific) or sialidase A (α2‐3 and α2‐6 specific). Data were obtained from the 50% acetonitrile fraction and all molecular ions are present in sodiated form ([M+Na]+). Sialylated species are annotated in red and those with GalαGal are annotated in blue.

Mentions: The proportion of α2‐3‐ versus α2‐6‐linked Sia present in the N‐glycans of porcine lung was further investigated by comparing sensitivity to digestion with linkage‐specific sialidases and control samples without sialidase treatment (Figure 2). Sialidase S was used for the specific release of α2‐3‐linked Sia, and Sialidase A for release of both α2‐3‐ and α2‐6‐linked Sia. The MALDI‐TOF spectra of porcine lung N‐glycans are shown after digestion with Sialidase S (Figure 2B), Sialidase A (Figure 2C), and control undigested (Figure 2A). Digestion of the pig lung N‐glycans with Sialidase A (Figure 2C, Table S1) caused a complete loss of all Sia‐containing glycans (e.g. m/z 2605·3, 2635·3, 2809·4, 2839·4, 2966·5, 3054·5, 3084·5, 3258·4, 3462·6, 3492·6, and 4146·1). Concurrent with these observations, the glycans at m/z 2244·0 (Hex5HexNAc4Fuc), 2448·1 (Hex6HexNAc4Fuc), 2693·2 (Hex6HexNAc5Fuc1), 3101·4 (Hex8HexNAc5Fuc), 3346·9 (Hex8HexNAc6Fuc), 3550·6 (Hex9HexNAc6Fuc), and 3754·6 (Hex10HexNAc6Fuc), which would be produced by de‐sialylating the above glycans, increased in abundance after Sialidase A treatment, confirming the presence of Sia‐containing N‐glycans in the pig lung. By contrast, digestion of the pig lung N‐glycans with Sialidase S (Figure 2B) caused a partial loss of Sia‐containing glycans with signals at m/z 2605·5, 2636·5, 2809·6, 2839·6, 3054·7, 3084·7, 3462·9, 3942·9, and 4146·3 still remaining. This confirmed that pig lung N‐glycans contained both α2‐3‐ and α2‐6‐linked Sia.


Infection of swine ex vivo tissues with avian viruses including H7N9 and correlation with glycomic analysis.

Chan RW, Karamanska R, Van Poucke S, Van Reeth K, Chan IW, Chan MC, Dell A, Peiris JS, Haslam SM, Guan Y, Nicholls JM - Influenza Other Respir Viruses (2013)

N‐glycan profile of swine lung following sialidase treatment. Partial MALDI‐TOF MS profiles of the permethylated N‐linked glycans derived from swine trachea after digestion with sialidase S (α2‐3 specific) or sialidase A (α2‐3 and α2‐6 specific). Data were obtained from the 50% acetonitrile fraction and all molecular ions are present in sodiated form ([M+Na]+). Sialylated species are annotated in red and those with GalαGal are annotated in blue.
© Copyright Policy - creativeCommonsBy-nc
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4114536&req=5

irv12144-fig-0002: N‐glycan profile of swine lung following sialidase treatment. Partial MALDI‐TOF MS profiles of the permethylated N‐linked glycans derived from swine trachea after digestion with sialidase S (α2‐3 specific) or sialidase A (α2‐3 and α2‐6 specific). Data were obtained from the 50% acetonitrile fraction and all molecular ions are present in sodiated form ([M+Na]+). Sialylated species are annotated in red and those with GalαGal are annotated in blue.
Mentions: The proportion of α2‐3‐ versus α2‐6‐linked Sia present in the N‐glycans of porcine lung was further investigated by comparing sensitivity to digestion with linkage‐specific sialidases and control samples without sialidase treatment (Figure 2). Sialidase S was used for the specific release of α2‐3‐linked Sia, and Sialidase A for release of both α2‐3‐ and α2‐6‐linked Sia. The MALDI‐TOF spectra of porcine lung N‐glycans are shown after digestion with Sialidase S (Figure 2B), Sialidase A (Figure 2C), and control undigested (Figure 2A). Digestion of the pig lung N‐glycans with Sialidase A (Figure 2C, Table S1) caused a complete loss of all Sia‐containing glycans (e.g. m/z 2605·3, 2635·3, 2809·4, 2839·4, 2966·5, 3054·5, 3084·5, 3258·4, 3462·6, 3492·6, and 4146·1). Concurrent with these observations, the glycans at m/z 2244·0 (Hex5HexNAc4Fuc), 2448·1 (Hex6HexNAc4Fuc), 2693·2 (Hex6HexNAc5Fuc1), 3101·4 (Hex8HexNAc5Fuc), 3346·9 (Hex8HexNAc6Fuc), 3550·6 (Hex9HexNAc6Fuc), and 3754·6 (Hex10HexNAc6Fuc), which would be produced by de‐sialylating the above glycans, increased in abundance after Sialidase A treatment, confirming the presence of Sia‐containing N‐glycans in the pig lung. By contrast, digestion of the pig lung N‐glycans with Sialidase S (Figure 2B) caused a partial loss of Sia‐containing glycans with signals at m/z 2605·5, 2636·5, 2809·6, 2839·6, 3054·7, 3084·7, 3462·9, 3942·9, and 4146·3 still remaining. This confirmed that pig lung N‐glycans contained both α2‐3‐ and α2‐6‐linked Sia.

Bottom Line: There was a greater abundance of Gal-α-Gal linkages resulting in a relative decrease in sialylated glycans.The swine respiratory tract also had a greater proportion of glycans containing Neu5Gc and Siaα2-6 glycans than the human respiratory tract.In contrast to previous studies we found that there was not as much expression of Siaα2-3 glycans on the surface of the trachea.

View Article: PubMed Central - PubMed

Affiliation: Department of Pathology, School of Public Health, Li Ka Shing Faculty of Medicine, The University of Hong Kong, Pokfulam, Hong Kong SAR, China; Centre of Influenza Research, School of Public Health, Li Ka Shing Faculty of Medicine, The University of Hong Kong, Pokfulam, Hong Kong SAR, China.

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Related in: MedlinePlus