dc.contributor.author | Mayr, Juliane | |
dc.contributor.author | Lau, Kam | |
dc.contributor.author | Lai, Jimmy CC | |
dc.contributor.author | Gagarinov, Ivan A | |
dc.contributor.author | Shi, Yun | |
dc.contributor.author | McAtamney, Sarah | |
dc.contributor.author | Chan, Renee WY | |
dc.contributor.author | Nicholls, John | |
dc.contributor.author | von Itzstein, Mark | |
dc.contributor.author | Haselhorst, Thomas | |
dc.date.accessioned | 2019-05-29T13:16:07Z | |
dc.date.available | 2019-05-29T13:16:07Z | |
dc.date.issued | 2018 | |
dc.identifier.issn | 2045-2322 | |
dc.identifier.doi | 10.1038/s41598-018-34175-3 | |
dc.identifier.uri | http://hdl.handle.net/10072/382119 | |
dc.description.abstract | The initial stage of host cell infection by influenza A viruses (IAV) is mediated through interaction of
the viral haemagglutinin (HA) with cell surface glycans. The binding requirement of IAVs for Galβ(1,4)
Glc/ GlcNAc (lactose/lactosamine) glycans with a terminal α(2,6)-linked (human receptors) or α(2,3)-
linked (avian receptors) N-acetylneuraminic residue commonly found on N-glycans, is well-established.
However the role and significance of sialylated Galβ(1,3)GalNAc (core 1) epitopes that are typical Oglycoforms
in influenza virus pathogenesis remains poorly detailed. Here we report a multidisciplinary
study using NMR spectroscopy, virus neutralization assays and molecular modelling, into the potential
for IAV to engage sialyl-Galβ(1,3)GalNAc O-glycoforms for cell attachment. H5 containing virus like
particles (VLPs) derived from an H5N1 avian IAV strain show a significant involvement of the O-glycanspecific
GalNAc residue, coordinated by a EQTKLY motif conserved in highly pathogenic avian influenza
(HPAI) strains. Notably, human pandemic H1N1 influenza viruses shift the preference from ‘humanlike’
α(2,6)-linkages in sialylated Galβ(1,4)Glc/GlcNAc fragments to ‘avian-like’ α(2,3)-linkages in
sialylated Galβ(1,3)GalNAc without involvement of the GalNAc residue. Overall, our study suggests that
sialylated Galβ(1,3)GalNAc as O-glycan core 1 glycoforms are involved in the influenza A virus life cycle
and play a particularly crucial role during infection of HPAI strains. | |
dc.description.peerreviewed | Yes | |
dc.language | English | |
dc.language.iso | eng | |
dc.publisher | Nature Publishing Group | |
dc.publisher.place | United Kingdom | |
dc.relation.ispartofchapter | 16382 | |
dc.relation.ispartofpagefrom | 1 | |
dc.relation.ispartofpageto | 12 | |
dc.relation.ispartofjournal | Scientific Reports | |
dc.relation.ispartofvolume | 8 | |
dc.subject.fieldofresearch | Other biomedical and clinical sciences not elsewhere classified | |
dc.subject.fieldofresearch | Other health sciences not elsewhere classified | |
dc.subject.fieldofresearchcode | 329999 | |
dc.subject.fieldofresearchcode | 429999 | |
dc.title | Unravelling the Role of O-glycans in Influenza A Virus Infection | |
dc.type | Journal article | |
dc.type.description | C1 - Articles | |
dc.type.code | C - Journal Articles | |
dcterms.license | http://creativecommons.org/licenses/by/4.0/ | |
dc.description.version | Version of Record (VoR) | |
gro.faculty | Office of the Snr Dep Vice Chancellor, Institute for Glycomics | |
gro.rights.copyright | © The Author(s) 2018. This is an Open Access article distributed under the terms of the Creative Commons Attribution 4.0 International (http://creativecommons.org/licenses/by/4.0/) which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. | |
gro.hasfulltext | Full Text | |
gro.griffith.author | von Itzstein, Mark | |
gro.griffith.author | Haselhorst, Thomas E. | |
gro.griffith.author | Shi, Yun | |