tetano
Editor, Senior Moderator
Proc Natl Acad Sci U S A. 2014 May 19. pii: 201323162. [Epub ahead of print]
Shotgun glycomics of pig lung identifies natural endogenous receptors for influenza viruses.
Byrd-Leotis L1, Liu R2, Bradley KC1, Lasanajak Y2, Cummings SF3, Song X2, Heimburg-Molinaro J2, Galloway SE1, Culhane MR4, Smith DF2, Steinhauer DA5, Cummings RD6.
Author information
Abstract
Influenza viruses bind to host cell surface glycans containing terminal sialic acids, but as studies on influenza binding become more sophisticated, it is becoming evident that although sialic acid may be necessary, it is not sufficient for productive binding. To better define endogenous glycans that serve as viral receptors, we have explored glycan recognition in the pig lung, because influenza is broadly disseminated in swine, and swine have been postulated as an intermediary host for the emergence of pandemic strains. For these studies, we used the technology of "shotgun glycomics" to identify natural receptor glycans. The total released N- and O-glycans from pig lung glycoproteins and glycolipid-derived glycans were fluorescently tagged and separated by multidimensional HPLC, and individual glycans were covalently printed to generate pig lung shotgun glycan microarrays. All viruses tested interacted with one or more sialylated N-glycans but not O-glycans or glycolipid-derived glycans, and each virus demonstrated novel and unexpected differences in endogenous N-glycan recognition. The results illustrate the repertoire of specific, endogenous N-glycans of pig lung glycoproteins for virus recognition and offer a new direction for studying endogenous glycan functions in viral pathogenesis.
KEYWORDS:
hemagglutinin, receptor binding, virus attachment
PMID:
24843157
[PubMed - as supplied by publisher]
http://www.ncbi.nlm.nih.gov/pubmed/24843157
Shotgun glycomics of pig lung identifies natural endogenous receptors for influenza viruses.
Byrd-Leotis L1, Liu R2, Bradley KC1, Lasanajak Y2, Cummings SF3, Song X2, Heimburg-Molinaro J2, Galloway SE1, Culhane MR4, Smith DF2, Steinhauer DA5, Cummings RD6.
Author information
Abstract
Influenza viruses bind to host cell surface glycans containing terminal sialic acids, but as studies on influenza binding become more sophisticated, it is becoming evident that although sialic acid may be necessary, it is not sufficient for productive binding. To better define endogenous glycans that serve as viral receptors, we have explored glycan recognition in the pig lung, because influenza is broadly disseminated in swine, and swine have been postulated as an intermediary host for the emergence of pandemic strains. For these studies, we used the technology of "shotgun glycomics" to identify natural receptor glycans. The total released N- and O-glycans from pig lung glycoproteins and glycolipid-derived glycans were fluorescently tagged and separated by multidimensional HPLC, and individual glycans were covalently printed to generate pig lung shotgun glycan microarrays. All viruses tested interacted with one or more sialylated N-glycans but not O-glycans or glycolipid-derived glycans, and each virus demonstrated novel and unexpected differences in endogenous N-glycan recognition. The results illustrate the repertoire of specific, endogenous N-glycans of pig lung glycoproteins for virus recognition and offer a new direction for studying endogenous glycan functions in viral pathogenesis.
KEYWORDS:
hemagglutinin, receptor binding, virus attachment
PMID:
24843157
[PubMed - as supplied by publisher]
http://www.ncbi.nlm.nih.gov/pubmed/24843157