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Polysialic acid is a cellular receptor for human adenovirus 52
Umeå University, Faculty of Medicine, Department of Clinical Microbiology, Virology.
Umeå University, Faculty of Medicine, Department of Clinical Microbiology, Virology.
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2018 (English)In: Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, E-ISSN 1091-6490, Vol. 115, no 18, p. E4264-E4273Article in journal (Refereed) Published
Abstract [en]

Human adenovirus 52 (HAdV-52) is one of only three known HAdVs equipped with both a long and a short fiber protein. While the long fiber binds to the coxsackie and adenovirus receptor, the function of the short fiber in the virus life cycle is poorly understood. Here, we show, by glycan microarray analysis and cellular studies, that the short fiber knob (SFK) of HAdV-52 recognizes long chains of α-2,8-linked polysialic acid (polySia), a large posttranslational modification of selected carrier proteins, and that HAdV-52 can use polySia as a receptor on target cells. X-ray crystallography, NMR, molecular dynamics simulation, and structure-guided mutagenesis of the SFK reveal that the nonreducing, terminal sialic acid of polySia engages the protein with direct contacts, and that specificity for polySia is achieved through subtle, transient electrostatic interactions with additional sialic acid residues. In this study, we present a previously unrecognized role for polySia as a cellular receptor for a human viral pathogen. Our detailed analysis of the determinants of specificity for this interaction has general implications for protein-carbohydrate interactions, particularly concerning highly charged glycan structures, and provides interesting dimensions on the biology and evolution of members of Human mastadenovirus G.

Place, publisher, year, edition, pages
2018. Vol. 115, no 18, p. E4264-E4273
Keywords [en]
human adenovirus, short fiber, polysialic acid, glycan receptor, glycan microarray
National Category
Structural Biology Microbiology in the medical area
Identifiers
URN: urn:nbn:se:umu:diva-147815DOI: 10.1073/pnas.1716900115ISI: 000431119600017PubMedID: 29674446OAI: oai:DiVA.org:umu-147815DiVA, id: diva2:1209302
Available from: 2018-05-22 Created: 2018-05-22 Last updated: 2018-06-09Bibliographically approved

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Lenman, AnnasaraFrängsmyr, LarsPodgorski, Iva I.Arnberg, Niklas

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