Crystal structure of the fibre head domain of the Atadenovirus snake Adenovirus 1

DOI: 10.1371/journal.pone.0114373
PMID: 25486282

Authors: Abhimanyu K. Singh (Centro Nacional de Biotecnologia (CNB-CSIC)) , Rosa Menéndez-Conejero (Centro Nacional de Biotecnologia (CNB-CSIC)) , Carmen San Martín (Centro Nacional de Biotecnologia (CNB-CSIC)) , Mark J. Van Raaij (Centro Nacional de Biotecnologia (CNB-CSIC)) , Eric J. Kremer (Centro Nacional de Biotecnologia (CNB-CSIC))
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Plos One , VOL 9 (12)

State: Published (Approved)
Published: December 2014
Diamond Proposal Number(s): 3808

Abstract: Adenoviruses are non-enveloped icosahedral viruses with trimeric fibre proteins protruding from their vertices. There are five known genera, from which only Mastadenoviruses have been widely studied. Apart from studying adenovirus as a biological model system and with a view to prevent or combat viral infection, there is a major interest in using adenovirus for vaccination, cancer therapy and gene therapy purposes. Adenoviruses from the Atadenovirus genus have been isolated from squamate reptile hosts, ruminants and birds and have a characteristic gene organization and capsid morphology. The carboxy-terminal virus-distal fibre head domains are likely responsible for primary receptor recognition. We determined the high-resolution crystal structure of the Snake Adenovirus 1 (SnAdV-1) fibre head using the multi-wavelength anomalous dispersion (MAD) method. Despite the absence of significant sequence homology, this Atadenovirus fibre head has the same beta-sandwich propeller topology as other adenovirus fibre heads. However, it is about half the size, mainly due to much shorter loops connecting the beta-strands. The detailed structure of the SnAdV-1 fibre head and other animal adenovirus fibre heads, together with the future identification of their natural receptors, may lead to the development of new strategies to target adenovirus vectors to cells of interest.

Journal Keywords: Adenoviruses; Crystal structure; Monomers; Crystal structure refinement; Protein structure; Viral structure; Crystals; Crystallization

Diamond Keywords: Viruses

Subject Areas: Biology and Bio-materials


Instruments: I02-Macromolecular Crystallography

Other Facilities: BM14, ID14-EH4, ID29 at ESRF

Added On: 17/12/2014 13:03

Discipline Tags:

Pathogens Infectious Diseases Health & Wellbeing Structural biology Life Sciences & Biotech

Technical Tags:

Diffraction Macromolecular Crystallography (MX)