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10.1080/07391102.2020.1851303

http://scihub22266oqcxt.onion/10.1080/07391102.2020.1851303
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suck abstract from ncbi


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pmid33292056      J+Biomol+Struct+Dyn 2022 ; 40 (9): 3880-3898
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  • Sensing the interactions between carbohydrate-binding agents and N-linked glycans of SARS-CoV-2 spike glycoprotein using molecular docking and simulation studies #MMPMID33292056
  • Lokhande KB; Apte GR; Shrivastava A; Singh A; Pal JK; K Venkateswara Swamy; Gupta RK
  • J Biomol Struct Dyn 2022[Jun]; 40 (9): 3880-3898 PMID33292056show ga
  • A recent surge in finding new candidate vaccines and potential antivirals to tackle atypical pneumonia triggered by the novel severe acute respiratory syndrome coronavirus-2 (SARS-CoV-2) needs new and unexplored approaches in solving this global pandemic. The homotrimeric transmembrane spike (S) glycoprotein of coronaviruses which facilitates virus entry into the host cells is covered with N-linked glycans having oligomannose and complex sugars. These glycans provide a unique opportunity for their targeting via carbohydrate-binding agents (CBAs) which have shown their antiviral potential against coronaviruses and enveloped viruses. However, CBA-ligand interaction is not fully explored in developing novel carbohydrate-binding-based antivirals due to associated unfavorable responses with CBAs. CBAs possess unique carbohydrate-binding specificity, therefore, CBAs like mannose-specific plant lectins/lectin-like mimic Pradimicin-A (PRM-A) can be used for targeting N-linked glycans of S glycoproteins. Here, we report studies on the binding and stability of lectins (NPA, UDA, GRFT, CV-N and wild-type and mutant BanLec) and PRM-A with the S glycoprotein glycans via docking and MD simulation. MM/GBSA calculations were also performed for docked complexes. Interestingly, stable BanLec mutant (H84T) also showed similar docking affinity and interactions as compared to wild-type BanLec, thus, confirming that uncoupling the mitogenic activity did not alter the lectin binding activity of BanLec. The stability of the docked complexes, i.e. PRM-A and lectins with SARS-CoV-2 S glycoprotein showed favorable intermolecular hydrogen-bond formation during the 100 ns MD simulation. Taking these together, our predicted in silico results will be helpful in the design and development of novel CBA-based antivirals for the SARS-CoV-2 neutralization.Communicated by Ramaswamy H. Sarma.
  • |*Antiviral Agents/chemistry[MESH]
  • |*SARS-CoV-2/drug effects[MESH]
  • |*Spike Glycoprotein, Coronavirus/chemistry[MESH]
  • |COVID-19[MESH]
  • |Glycoproteins[MESH]
  • |Humans[MESH]
  • |Lectins[MESH]
  • |Molecular Docking Simulation[MESH]


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