Using cryo-electron microscopy, structural features of feline infectious peritonitis virus (FIPV) can provide valuable information to understand the pathogenesis of infection.
To better understand the molecular basis of feline infectious peritonitis (FIP), Dr Danny Hsu Shang-Te from the Institute of Biological Chemistry, Academia Sinica, together with Dr Khoo Kay-Hooi and Professor Chang Hui-Wen and Professor Chang Yen-Chen from the Institute of Molecular and Comparative Pathobiology, College of Bioresources and Agriculture, National Taiwan University (NTU).
The team carried out an interdisciplinary investigation on the structure and function of the spike protein of type 1 FIPV. The spike protein of the virus is an essential target because it is used to recognize specific host cells and helps facilitate viral entry, which represents the first step of viral infection.
In the study published on PNAS, the researchers used cryo-electron microscopy from Academia Sinica to determine a high-resolution model of the spike protein of FIPV. Other methods employed were advanced biophysical and mass spectrometry techniques to elucidate complex post-translationally modified glycation structures that were directly visualized by cryo-electron microscopy single-molecule structure reconstruction analysis.
This molecular model revealed how the spike protein structure is densely decorated by the glycan components is able to evade the host immune system. These glycans may also play an essential role in host recognition.
With greater knowledge of the molecular structure of the spike proteins of FIPV will provide mechanistic understanding of FIP pathogenesis and broaden the underlying mechanism of coronavirus infection.
The researchers hope that this study will facilitate vaccine design for FIPV and also diagnosis methods of FIPV. [APBN]