TY  - JOUR
N1  - The copyroght of this article belongs to Elsevier
ID  - open3060
UR  - https://www.sciencedirect.com/science/article/pii/S016817022200096X?via%3Dihub
A1  - Sarkar, Anindya
A1  - Paul, Sathi
A1  - Singh, Charandeep
A1  - Chowdhury, Nilkanta
A1  - Nag, Papri
A1  - Das, Swarnava
A1  - Kumar, Sahil
A1  - Sharma, Anshul
A1  - Das, Deepjyoti Kumar
A1  - Dutta, Dipak
A1  - Thakur, Krishan Gopal
A1  - Bagchi, Angshuman
A1  - Shriti, Surbhi
A1  - Das, Kali P.
A1  - Ringe, Rajesh P.
A1  - Das, Sampa
Y1  - 2022/07/02/
N2  - COVID-19 caused by SARS-CoV-2 virus has had profound impact on the world in the past two years. Intense research is going on to find effective drugs to combat the disease. Over the past year several vaccines were approved for immunization. But SARS-CoV-2 being an RNA virus is continuously mutating to generate new variants, some of which develop features of immune escape. This raised serious doubts over the long-term efficacy of the vaccines. We have identified a unique mannose binding plant lectin from Narcissus tazetta bulb, NTL-125, which effectively inhibits SARS-CoV-2 replication in Vero-E6 cell line. In silico docking studies revealed that NTL-125 has strong affinity to viral Spike RBD protein, preventing it from attaching to hACE2 receptor, the gateway to cellular entry. Binding analyses revealed that all the mutant variants of Spike protein also have stronger affinity for NTL-125 than hACE2. The unique ?-helical tail of NTL-125 plays most important role in binding to RBD of Spike. NTL-125 also interacts effectively with some glycan moieties of S-protein in addition to amino acid residues adding to the binding strength. Thus, NTL-125 is a highly potential antiviral compound of natural origin against SARS-CoV-2 and may serve as an important therapeutic for management of COVID-19.
PB  - Elsevier
JF  - VIRUS RESEARCH
VL  - 315
KW  - Molecular docking; Mutant variants
KW  -  Narcissus tazetta lectin; SARS-CoV-2; Spike Protein
TI  - A novel plant lectin, NTL-125, interferes with SARS-CoV-2 interaction with hACE2
ER  -