AsianScientist (Sep. 13, 2016) – An international group of scientists has solved the atomic structure of the human aichi virus (AiV), a rather unusual but poorly characterized picornavirus that is very common and can cause severe gastroenteritis in children. Their work was published in Nature Microbiology.
Acute viral gastroenteritis is a leading cause of morbidity worldwide and an important cause of death in children less than five years old, especially in developing countries. Once a human is infected, AiV can lead to acute gastroenteritis. The seroprevalance (the level of a pathogen in a population as measured in blood serum) of AiV is approximately 60 percent in children under the age of ten years and reaches 90 percent later in life.
Professor Rao Zihe and Professor Wang Xiangxi of the Institute of Biophysics, the Chinese Academy of Sciences in China, together with colleagues in the UK, used cryo-electron microscopy to determine the atomic structure of this elusive virus at 3.68 angstrom resolution.
The structure showed that a highly exposed polyproline helix at the C-terminus of VP1 acts as a recognition motif for binding to the host enteric receptor. This would imply a mode of engagement with the host cell unlike others described for picornaviruses.
In addition, the researchers found the interactions between pentamers determine viral particle stability, suggesting that enhancing these interactions would be a target for the rational design of a picornavirus vaccine to improve its stability.
The article can be found at: Zhu et al. (2016) Structure of Human Aichi Virus and Implications for Receptor Binding.
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Source: Chinese Academy of Sciences; Photo: Shutterstock.
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