PMID- 32511307
OWN - NLM
STAT- PubMed-not-MEDLINE
LR  - 20240216
DP  - 2020 May 1
TI  - Analysis of the SARS-CoV-2 spike protein glycan shield: implications for immune 
      recognition.
LID - 2020.04.07.030445 [pii]
LID - 10.1101/2020.04.07.030445 [doi]
AB  - Here we have generated 3D structures of glycoforms of the spike (S) glycoprotein 
      from SARS-CoV-2, based on reported 3D structures and glycomics data for the 
      protein produced in HEK293 cells. We also analyze structures for glycoforms 
      representing those present in the nascent glycoproteins (prior to enzymatic 
      modifications in the Golgi), as well as those that are commonly observed on 
      antigens present in other viruses. These models were subjected to molecular 
      dynamics (MD) simulation to determine the extent to which glycan 
      microheterogeneity impacts the antigenicity of the S glycoprotein. Lastly, we 
      have identified peptides in the S glycoprotein that are likely to be presented in 
      human leukocyte antigen (HLA) complexes, and discuss the role of S protein 
      glycosylation in potentially modulating the adaptive immune response to the 
      SARS-CoV-2 virus or to a related vaccine. The 3D structures show that the protein 
      surface is extensively shielded from antibody recognition by glycans, with the 
      exception of the ACE2 receptor binding domain, and also that the degree of 
      shielding is largely insensitive to the specific glycoform. Despite the 
      relatively modest contribution of the glycans to the total molecular weight (17% 
      for the HEK293 glycoform) the level of surface shielding is disproportionately 
      high at 42%.
FAU - Grant, Oliver C
AU  - Grant OC
AD  - Complex Carbohydrate Research Center, University of Georgia, 315 Riverbend Rd, 
      Athens, GA 30602.
FAU - Montgomery, David
AU  - Montgomery D
AD  - Complex Carbohydrate Research Center, University of Georgia, 315 Riverbend Rd, 
      Athens, GA 30602.
FAU - Ito, Keigo
AU  - Ito K
AD  - Complex Carbohydrate Research Center, University of Georgia, 315 Riverbend Rd, 
      Athens, GA 30602.
FAU - Woods, Robert J
AU  - Woods RJ
AD  - Complex Carbohydrate Research Center, University of Georgia, 315 Riverbend Rd, 
      Athens, GA 30602.
LA  - eng
GR  - P41 GM103390/GM/NIGMS NIH HHS/United States
GR  - U01 CA207824/CA/NCI NIH HHS/United States
PT  - Preprint
DEP - 20200501
PL  - United States
TA  - bioRxiv
JT  - bioRxiv : the preprint server for biology
JID - 101680187
UIN - Sci Rep. 2020 Sep 14;10(1):14991. PMID: 32929138
PMC - PMC7217288
COIS- Competing Interests The authors declare no competing interests.
EDAT- 2020/06/09 06:00
MHDA- 2020/06/09 06:01
PMCR- 2020/05/12
CRDT- 2020/06/09 06:00
PHST- 2020/06/09 06:00 [entrez]
PHST- 2020/06/09 06:00 [pubmed]
PHST- 2020/06/09 06:01 [medline]
PHST- 2020/05/12 00:00 [pmc-release]
AID - 2020.04.07.030445 [pii]
AID - 10.1101/2020.04.07.030445 [doi]
PST - epublish
SO  - bioRxiv [Preprint]. 2020 May 1:2020.04.07.030445. doi: 10.1101/2020.04.07.030445.