Publication

Article Metrics

Citations


Online attention

Structure of human Aichi virus and implications for receptor binding

DOI: 10.1038/nmicrobiol.2016.150 DOI Help

Authors: Ling Zhu (University of Oxford; The Pirbright Institute) , Xiangxi Wang (Chinese Academy of Science) , Jingshan Ren (University of Oxford) , Abhay Kotecha (University of Oxford) , Thomas S. Walter (University of Oxford) , Shuai Yuan (Chinese Academy of Science) , Teruo Yamashita (Aichi Prefectural Institute of Public Health) , Tobias J. Tuthill (The Pirbright Institute) , Elizabeth E. Fry (University of Oxford) , Zihe Rao (Chinese Academy of Science; Tsinghua University) , David I. Stuart (Diamond Light Source; University of Oxford)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Nature Microbiology , VOL 1

State: Published (Approved)
Published: September 2016

Abstract: Aichi virus (AiV), an unusual and poorly characterized picornavirus, classified in the genus Kobuvirus, can cause severe gastroenteritis and deaths in children below the age of five years, especially in developing countries1,2. The seroprevalence of AiV is approximately 60% in children under the age of ten years and reaches 90% later in life3,4. There is no available vaccine or effective antiviral treatment. Here, we describe the structure of AiV at 3.7 Å. This first high-resolution structure for a kobuvirus is intermediate between those of the enteroviruses and cardioviruses, with a shallow, narrow depression bounded by the prominent VP0 CD loops (linking the C and D strands of the β-barrel), replacing the depression known as the canyon, frequently the site of receptor attachment in enteroviruses. VP0 is not cleaved to form VP2 and VP4, so the ‘VP2’ β-barrel structure is complemented with a unique extended structure on the inside of the capsid. On the outer surface, a polyproline helix structure, not seen previously in picornaviruses is present at the C terminus of VP1, a position where integrin binding motifs are found in some other picornaviruses. A peptide corresponding to this polyproline motif somewhat attenuates virus infectivity, presumably blocking host-cell attachment. This may guide cellular receptor identification.

Journal Keywords: Cryoelectron microscopy; Gastroenteritis; Virus–host interactions; Virus structures

Subject Areas: Biology and Bio-materials, Medicine


Technical Areas: