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Structure and N-acetylglucosamine binding of the distal domain of mouse adenovirus 2 fibre

Singh, Abhimanyu K., Nguyen, Thanh H., Vidovszky, Márton Z., Harrach, Balázs, Benk?, Mária, Kirwan, Alan, Joshi, Lokesh, Kilcoyne, Michelle, Berbis, M. Álvaro, Cañada, F. Javier, and others. (2018) Structure and N-acetylglucosamine binding of the distal domain of mouse adenovirus 2 fibre. Journal of General Virology, . ISSN 1465-2099. (doi:10.1099/jgv.0.001145) (The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided) (KAR id:69534)

The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided. (Contact us about this Publication)
Official URL
https://dx.doi.org/10.1099/jgv.0.001145

Abstract

Murine adenovirus 2 (MAdV-2) infects cells of the mouse gastrointestinal tract. Like human adenoviruses, it is a member of the genus Mastadenovirus, family Adenoviridae. The MAdV-2 genome has a single fibre gene that expresses a 787 residue-long protein. Through analogy to other adenovirus fibre proteins, it is expected that the carboxy-terminal virus-distal head domain of the fibre is responsible for binding to the host cell, although the natural receptor is unknown. The putative head domain has little sequence identity to adenovirus fibres of known structure. In this report, we present high-resolution crystal structures of the carboxy-terminal part of the MAdV-2 fibre. The structures reveal a domain with the typical adenovirus fibre head topology and a domain containing two triple ?-spiral repeats of the shaft domain. Through glycan microarray profiling, saturation transfer difference nuclear magnetic resonance spectroscopy, isothermal titration calorimetry and site-directed mutagenesis, we show that the fibre specifically binds to the monosaccharide N-acetylglucosamine (GlcNAc). The crystal structure of the complex reveals that GlcNAc binds between the AB and CD loops at the top of each of the three monomers of the MAdV-2 fibre head. However, infection competition assays show that soluble GlcNAc monosaccharide and natural GlcNAc-containing polymers do not inhibit infection by MAdV-2. Furthermore, site-directed mutation of the GlcNAc-binding residues does not prevent the inhibition of infection by soluble fibre protein. On the other hand, we show that the MAdV-2 fibre protein binds GlcNAc-containing mucin glycans, which suggests that the MAdV-2 fibre protein may play a role in viral mucin penetration in the mouse gut.

Item Type: Article
DOI/Identification number: 10.1099/jgv.0.001145
Uncontrolled keywords: Virology
Divisions: Faculties > Sciences > School of Biosciences
SWORD Depositor: JISC Publications Router
Depositing User: Abhimanyu Singh
Date Deposited: 18 Oct 2018 14:18 UTC
Last Modified: 29 May 2019 21:16 UTC
Resource URI: https://kar.kent.ac.uk/id/eprint/69534 (The current URI for this page, for reference purposes)
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