On the interactions of the receptor-binding domain of SARS-CoV-1 and SARS-CoV-2 spike proteins with monoclonal antibodies and the receptor ACE2
This article has been Reviewed by the following groups
Listed in
- Evaluated articles (ScreenIT)
Abstract
No abstract available
Article activity feed
-
-
SciScore for 10.1101/2020.04.05.026377: (What is this?)
Please note, not all rigor criteria are appropriate for all manuscripts.
Table 1: Rigor
NIH rigor criteria are not applicable to paper type.Table 2: Resources
Software and Algorithms Sentences Resources The “UCSF Chimera 1.11.2” package45 was employed for all molecular visualizations and representations too. Chimerasuggested: (Chimera, RRID:SCR_002959)The pairwise sequence alignments were generated by the server EMBOSS Needle68 with default settings. EMBOSSsuggested: (EMBOSS, RRID:SCR_008493)Results from OddPub: Thank you for sharing your data.
Results from LimitationRecognizer: We detected the following sentences addressing limitations in the study:We are careful with the use of stronger statements here due to the limitation of the theoretical approach. Several additional issues remain to …
SciScore for 10.1101/2020.04.05.026377: (What is this?)
Please note, not all rigor criteria are appropriate for all manuscripts.
Table 1: Rigor
NIH rigor criteria are not applicable to paper type.Table 2: Resources
Software and Algorithms Sentences Resources The “UCSF Chimera 1.11.2” package45 was employed for all molecular visualizations and representations too. Chimerasuggested: (Chimera, RRID:SCR_002959)The pairwise sequence alignments were generated by the server EMBOSS Needle68 with default settings. EMBOSSsuggested: (EMBOSS, RRID:SCR_008493)Results from OddPub: Thank you for sharing your data.
Results from LimitationRecognizer: We detected the following sentences addressing limitations in the study:We are careful with the use of stronger statements here due to the limitation of the theoretical approach. Several additional issues remain to be further investigated. Finally, we compared the EE predictions for CR3022’ (34 aa) with CR3022 (33 aa) interacting with SARS-CoV-2 S RBD protein − see Figure 10. The predicted EEs for the interaction with CR3022’ are essentially the same ones observed for CR3022 (27 common aa). This implies that the suggested mutations here do not affected the antigenic regions. Another particularly interesting feature of this computer-designed molecule is that the number of EEs shared with ACE2 has increased from 18 (for CR3022) to 27 (for CR3022’). This might amplify the potential of this mAb candidate to better block the virus-host cell interaction.
Results from TrialIdentifier: No clinical trial numbers were referenced.
Results from Barzooka: We did not find any issues relating to the usage of bar graphs.
Results from JetFighter: We did not find any issues relating to colormaps.
Results from rtransparent:- No conflict of interest statement was detected. If there are no conflicts, we encourage authors to explicit state so.
- Thank you for including a funding statement. Authors are encouraged to include this statement when submitting to a journal.
- No protocol registration statement was detected.
-