Biochemical analysis of packing and assembling heptad repeat motifs in the coronavirus spike protein trimer.

ABSTRACT: During a coronavirus infection, the spike protein undergoes sequential structural transitions triggered by its receptor and the host protease at the interface between the virus and cell membranes, thereby mediating membrane fusion. After receptor binding, the heptad repeat motif (HR1/HR2) within the viral spike protein bridges the viral and cellular membranes; however, the intermediate conformation adopted by the spike protein when drawing the viral and cellular membranes into close proximity remains unclear due to its transient and unstable nature. Here, we experimentally induced conformational changes in the spike protein of a murine coronavirus by incubating the virus with its receptor, followed by exposure to trypsin. We then treated the virus/receptor complex with proteinase K to prob

SUBMITTER: Kobayashi J 

PROVIDER: S-EPMC11559096 | biostudies-literature | 2024 Nov

REPOSITORIES: biostudies-literature