Abstract
Sialic acids (Sias) are important glycans displayed on the cells and tissues of many different animals and are frequent targets for binding and modification by pathogens, including influenza viruses. Influenza virus hemagglutinins bind Sias during the infection of their normal hosts, while the encoded neuraminidases and/or esterases remove or modify the Sia to allow virion release or to prevent rebinding. Sias naturally occur in a variety of modified forms, and modified Sias can alter influenza virus host tropisms through their altered interactions with the viral glycoproteins. However, the distribution of modified Sia forms and their effects on pathogen-host interactions are still poorly understood. Here we used probes developed from viral Sia-binding proteins to detect O-acetylated (4-O-acetyl, 9-O-acetyl, and 7,9-O-acetyl) Sias displayed on the tissues of some natural or experimental hosts for influenza viruses. These modified Sias showed highly variable displays between the hosts and tissues examined. The 9-O-acetyl (and 7,9-) modified Sia forms were found on cells and tissues of many hosts, including mice, humans, ferrets, guinea pigs, pigs, horses, dogs, as well as in those of ducks and embryonated chicken egg tissues and membranes, although in variable amounts. The 4-O-acetyl Sias were found in the respiratory tissues of fewer animals, being primarily displayed in the horse and guinea pig, but were not detected in humans or pigs. The results suggest that these Sia variants may influence virus tropisms by altering and selecting their cell interactions.
| Original language | English (US) |
|---|---|
| Article number | e00379-16 |
| Journal | mSphere |
| Volume | 2 |
| Issue number | 5 |
| DOIs | |
| State | Published - Sep 1 2017 |
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Keywords
- Host range
- Influenza
- Receptor-ligand interaction
- Respiratory viruses
- Sialic acid
- Virus-host interactions
ASJC Scopus subject areas
- Microbiology
- Molecular Biology
Cite this
Distribution of O-acetylated sialic acids among target host tissues for influenza virus. / Wasik, Brian R.; Barnard, Karen N.; Ossiboff, Robert J.; Khedri, Zahra; Feng, Kurtis H.; Yu, Hai; Chen, Xi; Perez, Daniel R.; Varki, Ajit; Parrish, Colin R.
In: mSphere, Vol. 2, No. 5, e00379-16, 01.09.2017.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Distribution of O-acetylated sialic acids among target host tissues for influenza virus
AU - Wasik, Brian R.
AU - Barnard, Karen N.
AU - Ossiboff, Robert J.
AU - Khedri, Zahra
AU - Feng, Kurtis H.
AU - Yu, Hai
AU - Chen, Xi
AU - Perez, Daniel R.
AU - Varki, Ajit
AU - Parrish, Colin R.
PY - 2017/9/1
Y1 - 2017/9/1
N2 - Sialic acids (Sias) are important glycans displayed on the cells and tissues of many different animals and are frequent targets for binding and modification by pathogens, including influenza viruses. Influenza virus hemagglutinins bind Sias during the infection of their normal hosts, while the encoded neuraminidases and/or esterases remove or modify the Sia to allow virion release or to prevent rebinding. Sias naturally occur in a variety of modified forms, and modified Sias can alter influenza virus host tropisms through their altered interactions with the viral glycoproteins. However, the distribution of modified Sia forms and their effects on pathogen-host interactions are still poorly understood. Here we used probes developed from viral Sia-binding proteins to detect O-acetylated (4-O-acetyl, 9-O-acetyl, and 7,9-O-acetyl) Sias displayed on the tissues of some natural or experimental hosts for influenza viruses. These modified Sias showed highly variable displays between the hosts and tissues examined. The 9-O-acetyl (and 7,9-) modified Sia forms were found on cells and tissues of many hosts, including mice, humans, ferrets, guinea pigs, pigs, horses, dogs, as well as in those of ducks and embryonated chicken egg tissues and membranes, although in variable amounts. The 4-O-acetyl Sias were found in the respiratory tissues of fewer animals, being primarily displayed in the horse and guinea pig, but were not detected in humans or pigs. The results suggest that these Sia variants may influence virus tropisms by altering and selecting their cell interactions.
AB - Sialic acids (Sias) are important glycans displayed on the cells and tissues of many different animals and are frequent targets for binding and modification by pathogens, including influenza viruses. Influenza virus hemagglutinins bind Sias during the infection of their normal hosts, while the encoded neuraminidases and/or esterases remove or modify the Sia to allow virion release or to prevent rebinding. Sias naturally occur in a variety of modified forms, and modified Sias can alter influenza virus host tropisms through their altered interactions with the viral glycoproteins. However, the distribution of modified Sia forms and their effects on pathogen-host interactions are still poorly understood. Here we used probes developed from viral Sia-binding proteins to detect O-acetylated (4-O-acetyl, 9-O-acetyl, and 7,9-O-acetyl) Sias displayed on the tissues of some natural or experimental hosts for influenza viruses. These modified Sias showed highly variable displays between the hosts and tissues examined. The 9-O-acetyl (and 7,9-) modified Sia forms were found on cells and tissues of many hosts, including mice, humans, ferrets, guinea pigs, pigs, horses, dogs, as well as in those of ducks and embryonated chicken egg tissues and membranes, although in variable amounts. The 4-O-acetyl Sias were found in the respiratory tissues of fewer animals, being primarily displayed in the horse and guinea pig, but were not detected in humans or pigs. The results suggest that these Sia variants may influence virus tropisms by altering and selecting their cell interactions.
KW - Host range
KW - Influenza
KW - Receptor-ligand interaction
KW - Respiratory viruses
KW - Sialic acid
KW - Virus-host interactions
UR - http://www.scopus.com/inward/record.url?scp=85041528709&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=85041528709&partnerID=8YFLogxK
U2 - 10.1128/mSphere.00379-16
DO - 10.1128/mSphere.00379-16
M3 - Article
AN - SCOPUS:85041528709
VL - 2
JO - mSphere
JF - mSphere
SN - 2379-5042
IS - 5
M1 - e00379-16
ER -