Structural highlights
Publication Abstract from PubMedFeline infectious peritonitis virus (FIPV) is an alphacoronavirus that causes a nearly 100% mortality rate without effective treatment. Here we report a 3.3-A cryoelectron microscopy (cryo-EM) structure of the serotype I FIPV spike (S) protein, which is responsible for host recognition and viral entry. Mass spectrometry provided site-specific compositions of densely distributed high-mannose and complex-type N-glycans that account for 1/4 of the total molecular mass; most of the N-glycans could be visualized by cryo-EM. Specifically, the N-glycans that wedge between 2 galectin-like domains within the S1 subunit of FIPV S protein result in a unique propeller-like conformation, underscoring the importance of glycosylation in maintaining protein structures. The cleavage site within the S2 subunit responsible for activation also showed distinct structural features and glycosylation. These structural insights provide a blueprint for a better molecular understanding of the pathogenesis of FIP. Cryo-EM analysis of a feline coronavirus spike protein reveals a unique structure and camouflaging glycans.,Yang TJ, Chang YC, Ko TP, Draczkowski P, Chien YC, Chang YC, Wu KP, Khoo KH, Chang HW, Hsu SD Proc Natl Acad Sci U S A. 2020 Jan 21;117(3):1438-1446. doi:, 10.1073/pnas.1908898117. Epub 2020 Jan 3. PMID:31900356[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
| ||||||||||||||||||
This page was last modified 08:59, 5 February 2020.