Structure of a SARS-CoV-2 spike S2 subunit in a pre-fusion, open conformation.

ABSTRACT: The 800 million human infections with SARS-CoV-2 and the likely emergence of new variants and additional coronaviruses necessitate a better understanding of the essential spike glycoprotein and the development of immunogens that foster broader and more durable immunity. The S2 fusion subunit is more conserved in sequence, is essential to function, and would be a desirable immunogen to boost broadly reactive antibodies. It is, however, unstable in structure and in its wild-type form, cannot be expressed alone without irreversible collapse into a six-helix bundle. In addition to the irreversible conformational changes of fusion, biophysical measurements indicate that spike also undergoes a reversible breathing action. However, spike in an open, "breathing" conformation has not yet been visua

SUBMITTER: Olmedillas E 

PROVIDER: S-EPMC10760097 | biostudies-literature | 2023 Dec

REPOSITORIES: biostudies-literature