Author: So Young Kim; Weihua Jin; Amika Sood; David W. Montgomery; Oliver C. Grant; Mark M. Fuster; Li Fu; Jonathan S. Dordick; Robert J. Woods; Fuming Zhang; Robert J. Linhardt
Title: Glycosaminoglycan binding motif at S1/S2 proteolytic cleavage site on spike glycoprotein may facilitate novel coronavirus (SARS-CoV-2) host cell entry Document date: 2020_4_15
ID: fs8dn7ir_23
Snippet: GAG-protein interactions are mainly electrostatically driven [24] , thus, HS-binding proteins generally bind HP due to its higher degree of sulfation [15] . We discovered that HP binds both monomeric and trimeric SARS-CoV-2 SGP with remarkable affinity (KD = 40 pM and 73 pM, respectively) (Fig 2 and Table 1 ). This was unexpectedly tight binding for a GAG-protein interaction as even one of one of the prototypical HP-binding proteins, fibroblast g.....
Document: GAG-protein interactions are mainly electrostatically driven [24] , thus, HS-binding proteins generally bind HP due to its higher degree of sulfation [15] . We discovered that HP binds both monomeric and trimeric SARS-CoV-2 SGP with remarkable affinity (KD = 40 pM and 73 pM, respectively) (Fig 2 and Table 1 ). This was unexpectedly tight binding for a GAG-protein interaction as even one of one of the prototypical HP-binding proteins, fibroblast growth factor 2 (FGF2), has a KD of 39 nM [25] . In comparison, SARS-Cov and MERS-CoV SGPs also bind HP, author/funder. All rights reserved. No reuse allowed without permission.
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