Jesper Pallesen

TL;DR: An engineering strategy for stabilization of soluble S proteins in the prefusion conformation is described, which results in greatly increased expression, conformational homogeneity, and elicitation of potent antibody responses, and an engineered immunogen is able to elicit high neutralizing antibody titers against MERS-CoV.

TL;DR: Surprisingly, the S1 C-terminal domains are interdigitated and form extensive quaternary interactions that occlude surfaces known in other coronaviruses to bind protein receptors, which provide a structural basis to support a model of membrane fusion mediated by progressive S protein destabilization through receptor binding and proteolytic cleavage.

TL;DR: Cryo-EM analyses of a stabilized trimeric SARS-CoV S, as well as the trypsin-cleaved, stabilized S, and its interactions with ACE2 are presented, finding that neither binding to ACE2 nor cleavage bytrypsin at the S1/S2 cleavage site impart large conformational changes within stabilized SARV S.

TL;DR: This work presents a new analytical approach capable of determining the free-energy landscape and the continuous trajectories of molecular machines from a large number of snapshots obtained by cryogenic electron microscopy and allows model-free quantitative analysis of the degrees of freedom and the energy landscape underlying continuous conformational changes in nanomachines, including those important for biological function.

TL;DR: The most complete description yet, to the authors' knowledge, of the CD4–17b-induced intermediate is presented and provide the molecular basis of the receptor-binding-induced conformational change required for HIV-1 entry into host cells.