{"id":8701,"date":"2022-05-02T06:00:22","date_gmt":"2022-05-01T21:00:22","guid":{"rendered":"https:\/\/www.emukk.com\/WP\/?p=8701"},"modified":"2022-04-30T07:30:22","modified_gmt":"2022-04-29T22:30:22","slug":"a-unique-plant-lectin-from-narcissus-tazetta-bulb-ntl-125-could-effectively-inhibit-sars-cov-2-replication","status":"publish","type":"post","link":"https:\/\/www.emukk.com\/WP\/en\/a-unique-plant-lectin-from-narcissus-tazetta-bulb-ntl-125-could-effectively-inhibit-sars-cov-2-replication\/","title":{"rendered":"A unique plant lectin from Narcissus tazetta bulb, NTL-125, could effectively inhibit SARS-CoV-2 replication"},"content":{"rendered":"

A group from Division of Plant Biology, Bose Institute, P\/12 C.I.T. Scheme VII(M), Kolkata, 700054, India, etc. has reported that a unique mannose binding plant lectin from Narcissus tazetta bulb, NTL-125, could effectively inhibit SARS-CoV-2 replication in Vero-E6 cell line.
\nhttps:\/\/www.ncbi.nlm.nih.gov\/pmc\/articles\/PMC8988448\/<\/a><\/p>\n

A unique mannose binding plant lectin from Narcissus tazetta bulb named NTL-125 could inhibit SARS-CoV-2 replication in Vero-E6 cell line. The inhibitory concentration using Vero-E6 cells that reduced the SARS-CoV-2 viral entry by 50% (IC50<\/sub>) was approximately 0.8 \u00b5g\/mL (i.e., 50 nM), and the cytotoxicity of NLE-125 on Vero-E6 cells was above 95% viable at 5 \u00b5g\/mL and 85% viable at 10 \u00b5g\/mL concentration.<\/p>\n

The molecular docking studies revealed that thirty-six residues of RBD and 44 residues of NTL-125 were located within 5\u00c5 distance from each other in the complex whereas 27 residues of ACE-2 are in proximity to 32 residues of RBD. There are 17 common residues of RBD that interact with both ACE-2 and NTL-125. Among all these residues, for the RBD:NTL-125 complex, 10 of RBD and 11 of NTL-125 are within 3\u00c5 distance in the docked structure. For the RBD:ACE-2 complex, 9 residues of RBD and 9 residues of ACE-2 are within 3\u00c5 distance. NTL-125 occupies exactly the same region of the receptor binding motif (RBM) of the spike protein where hACE2 usually binds. As a result, the binding free energy change of NTL125\u2013Spike protein interaction (-13.3 kcal\/mol, kd ~0.41nM) is more negative than that between ACE2-Spike protein (-11.2 kcal\/mol, kd ~12 nM) which clearly indicates that the former is more stable than the later.<\/p>\n

Docking study confirmed further that the interaction between NTL-125-spike protein is also mediated through a S-protein glycan moiety, covalently linked to Asn165 of the spike protein and interacts with Ile137 and Thr138 of NTL-125 protein. Thus, the interaction between NTL-125-Spike is not only through amino acid residues but also through the glycan moieties.<\/p>\n

\"\"<\/a><\/p>\n","protected":false},"excerpt":{"rendered":"

A group from Division of Plant Biology, Bose Institute, P\/12 C.I.T. Scheme VII(M), Kolkata, 700054, India, etc<\/p><\/div>\n

\u7d9a\u304d\u3092\u8aad\u3080<\/a><\/p>\n","protected":false},"author":1,"featured_media":0,"comment_status":"closed","ping_status":"closed","sticky":false,"template":"","format":"standard","meta":{"footnotes":""},"categories":[70,7],"tags":[],"class_list":["post-8701","post","type-post","status-publish","format-standard","hentry","category-nature-en","category-technology-en"],"aioseo_notices":[],"aioseo_head":"\n\t\t\n\t\n\t\n\t\n\t\n\t\n\t\t\n\t\t\n\t\t\n\t\t\n\t\t\n\t\t\n\t\t\n\t\t\n\t\t\n\t\t\n\t\t\n\t\t\n\t\t\n\t\t\n\t\t