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Deprecated: Implicit conversion from float 265.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Front+Immunol 2021 ; 12 (ä): 660198 Nephropedia Template TP
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Enhancing the Prefusion Conformational Stability of SARS-CoV-2 Spike Protein Through Structure-Guided Design #MMPMID33968063
Riley TP; Chou HT; Hu R; Bzymek KP; Correia AR; Partin AC; Li D; Gong D; Wang Z; Yu X; Manzanillo P; Garces F
Front Immunol 2021[]; 12 (ä): 660198 PMID33968063show ga
The worldwide pandemic caused by the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is unprecedented and the impact on public health and the global economy continues to be devastating. Although early therapies such as prophylactic antibodies and vaccines show great promise, there are concerns about the long-term efficacy and universal applicability of these therapies as the virus continues to mutate. Thus, protein-based immunogens that can quickly respond to viral changes remain of continued interest. The Spike protein, the main immunogen of this virus, displays a highly dynamic trimeric structure that presents a challenge for therapeutic development. Here, guided by the structure of the Spike trimer, we rationally design new Spike constructs that show a uniquely high stability profile while simultaneously remaining locked into the immunogen-desirable prefusion state. Furthermore, our approach emphasizes the relationship between the highly conserved S2 region and structurally dynamic Receptor Binding Domains (RBD) to enable vaccine development as well as the generation of antibodies able to resist viral mutation.
|Angiotensin-Converting Enzyme 2/metabolism[MESH]
|Antibodies, Neutralizing/immunology[MESH]
|Antibodies, Viral/immunology[MESH]
|Binding Sites/genetics/immunology[MESH]
|COVID-19/immunology/pathology[MESH]
|Cell Line[MESH]
|HEK293 Cells[MESH]
|Humans[MESH]
|Protein Domains/genetics/immunology[MESH]
|Protein Interaction Domains and Motifs/*genetics/*immunology[MESH]