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.
N1 - Funding Information:
We thank Wendy Weichert, Brynn Lawrence, and other members of the laboratory for technical assistance and support. We further express thanks for services and support in tissue processing by members of the Baker Institute of Animal Health and Histology division at the Cornell University College of Veterinary Medicine. Other researchers providing tissue samples included John Nicholls (University of Hong Kong), Richard Webby (St. Jude Children's Research Hospital), Randy Albrecht and Nichole Bouvier (Mount Sinai Medical Center), and Natasza Kurpios (Cornell University). Support for this work was funded in part by CRIP (Center of Research in Influenza Pathogenesis), an NIAID-funded Center of Excellence in Influenza Research and Surveillance (CEIRS; contract HHSN272201400008C to D.R.P. and C.R.P.), NIH grant R01 GM080533-05 to C.R.P., and NIH Common Fund grant (U01CA199792) to A.V
Publisher Copyright:
© 2017 Wasik et al.
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
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U2 - 10.1128/mSphere.00379-16
DO - 10.1128/mSphere.00379-16
M3 - Article
C2 - 28904995
AN - SCOPUS:85041528709
VL - 2
JO - mSphere
JF - mSphere
SN - 2379-5042
IS - 5
M1 - e00379-16
ER -