tetano
Editor, Senior Moderator
Int J Mol Sci
. 2021 Jun 16;22(12):6462.
doi: 10.3390/ijms22126462.
More Is Always Better Than One: The N-Terminal Domain of the Spike Protein as Another Emerging Target for Hampering the SARS-CoV-2 Attachment to Host Cells
Sonia Di Gaetano[SUP] 1 2 [/SUP], Domenica Capasso[SUP] 2 3 [/SUP], Pietro Delre[SUP] 4 5 [/SUP], Luciano Pirone[SUP] 1 [/SUP], Michele Saviano[SUP] 2 4 [/SUP], Emilia Pedone[SUP] 1 2 [/SUP], Giuseppe Felice Mangiatordi[SUP] 4 [/SUP]
Affiliations
Abstract
Although the approved vaccines are proving to be of utmost importance in containing the Coronavirus disease 2019 (COVID-19) threat, they will hardly be resolutive as new severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2, a single-stranded RNA virus) variants might be insensitive to the immune response they induce. In this scenario, developing an effective therapy is still a dire need. Different targets for therapeutic antibodies and diagnostics have been identified, among which the SARS-CoV-2 spike (S) glycoprotein, particularly its receptor-binding domain, has been defined as crucial. In this context, we aim to focus attention also on the role played by the S N-terminal domain (S1-NTD) in the virus attachment, already recognized as a valuable target for neutralizing antibodies, in particular, building on a cavity mapping indicating the presence of two druggable pockets and on the recent literature hypothesizing the presence of a ganglioside-binding domain. In this perspective, we aim at proposing S1-NTD as a putative target for designing small molecules hopefully able to hamper the SARS-CoV-2 attachment to host cells.
Keywords: cavity mapping; galectin inhibitors; spike Protein.
. 2021 Jun 16;22(12):6462.
doi: 10.3390/ijms22126462.
More Is Always Better Than One: The N-Terminal Domain of the Spike Protein as Another Emerging Target for Hampering the SARS-CoV-2 Attachment to Host Cells
Sonia Di Gaetano[SUP] 1 2 [/SUP], Domenica Capasso[SUP] 2 3 [/SUP], Pietro Delre[SUP] 4 5 [/SUP], Luciano Pirone[SUP] 1 [/SUP], Michele Saviano[SUP] 2 4 [/SUP], Emilia Pedone[SUP] 1 2 [/SUP], Giuseppe Felice Mangiatordi[SUP] 4 [/SUP]
Affiliations
- PMID: 34208755
- DOI: 10.3390/ijms22126462
Abstract
Although the approved vaccines are proving to be of utmost importance in containing the Coronavirus disease 2019 (COVID-19) threat, they will hardly be resolutive as new severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2, a single-stranded RNA virus) variants might be insensitive to the immune response they induce. In this scenario, developing an effective therapy is still a dire need. Different targets for therapeutic antibodies and diagnostics have been identified, among which the SARS-CoV-2 spike (S) glycoprotein, particularly its receptor-binding domain, has been defined as crucial. In this context, we aim to focus attention also on the role played by the S N-terminal domain (S1-NTD) in the virus attachment, already recognized as a valuable target for neutralizing antibodies, in particular, building on a cavity mapping indicating the presence of two druggable pockets and on the recent literature hypothesizing the presence of a ganglioside-binding domain. In this perspective, we aim at proposing S1-NTD as a putative target for designing small molecules hopefully able to hamper the SARS-CoV-2 attachment to host cells.
Keywords: cavity mapping; galectin inhibitors; spike Protein.