Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Biochemistry 2021 ; 60 (27): 2153-2169 Nephropedia Template TP
gab.com Text
Twit Text FOAVip
Twit Text #
English Wikipedia
Site-Specific Steric Control of SARS-CoV-2 Spike Glycosylation #MMPMID34213308
Allen JD; Chawla H; Samsudin F; Zuzic L; Shivgan AT; Watanabe Y; He WT; Callaghan S; Song G; Yong P; Brouwer PJM; Song Y; Cai Y; Duyvesteyn HME; Malinauskas T; Kint J; Pino P; Wurm MJ; Frank M; Chen B; Stuart DI; Sanders RW; Andrabi R; Burton DR; Li S; Bond PJ; Crispin M
Biochemistry 2021[Jul]; 60 (27): 2153-2169 PMID34213308show ga
A central tenet in the design of vaccines is the display of native-like antigens in the elicitation of protective immunity. The abundance of N-linked glycans across the SARS-CoV-2 spike protein is a potential source of heterogeneity among the many different vaccine candidates under investigation. Here, we investigate the glycosylation of recombinant SARS-CoV-2 spike proteins from five different laboratories and compare them against S protein from infectious virus, cultured in Vero cells. We find patterns that are conserved across all samples, and this can be associated with site-specific stalling of glycan maturation that acts as a highly sensitive reporter of protein structure. Molecular dynamics simulations of a fully glycosylated spike support a model of steric restrictions that shape enzymatic processing of the glycans. These results suggest that recombinant spike-based SARS-CoV-2 immunogen glycosylation reproducibly recapitulates signatures of viral glycosylation.
free
free
free
Biochemistry 2021 ; 60 (27): 2153-2169
