Abstract Title
Feeding- and temperature-dependent accumulation of norovirus like particles in oysters
Presenter
Ayaka Takahashi-Okino, Japan Institute for Health Security
Co-Author(s)
Ayaka Takahashi-Okino1,2, Satoru Takeyama3, Takashi Kamaishi4, Kosuke Murakami1,2
1. Department of Diagnostic Testing and Technology Research, National Institute of Infectious Diseases, Japan Institute for Health Security, Japan
2. Department of Virology II, Japan Institute for Health Security, Japan
3. Akkeshi Oyster Hatchery, Japan
4. Resources enhancement promotion department, Fisheries Agency, Ministry of Agriculture, Forestry and Fisheries, Japan
Abstract Category
Food & Environmental Virology-I (Food)
Abstract
Human norovirus (HuNoV), a causative agent of acute gastroenteritis, has been recognized as the most prevalent pathogen leading to outbreaks of foodborne illness worldwide. Shellfish, particularly bivalves such as oysters, is one of the primary sources of HuNoV-associated foodborne illness. However, understanding how bivalves accumulate HuNoV is insufficient. In this study, we investigated the mechanism using Pacific oysters (Crassostrea gigas) and virus-like particles (VLP).
Juvenile oysters (about 5 mm shell length) placed in 12-well plates with artificial seawater were fed with HuNoV VLP in the presence or absence of diatoms (Chaetoceros gracilis) at either room temperature around 20°C or 4°C for 2 hours. After removing the shells, the wet weight of the whole body was measured and ground with a masher. Subsequently, the proteins extracted from the whole body were analyzed by western blotting to detect the capsid protein VP1 using VLP-specific antiserum.
Juvenile oysters (about 5 mm shell length) placed in 12-well plates with artificial seawater were fed with HuNoV VLP in the presence or absence of diatoms (Chaetoceros gracilis) at either room temperature around 20°C or 4°C for 2 hours. After removing the shells, the wet weight of the whole body was measured and ground with a masher. Subsequently, the proteins extracted from the whole body were analyzed by western blotting to detect the capsid protein VP1 using VLP-specific antiserum.