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Deprecated: Implicit conversion from float 245.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Sci+Rep 2020 ; 10 (1): 16944 Nephropedia Template TP
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The sequence at Spike S1/S2 site enables cleavage by furin and phospho-regulation in SARS-CoV2 but not in SARS-CoV1 or MERS-CoV #MMPMID33037310
Ord M; Faustova I; Loog M
Sci Rep 2020[Oct]; 10 (1): 16944 PMID33037310show ga
The Spike protein of the novel coronavirus SARS-CoV2 contains an insertion (680)SPRRAR downward arrowSV(687) forming a cleavage motif RxxR for furin-like enzymes at the boundary of S1/S2 subunits. Cleavage at S1/S2 is important for efficient viral entry into target cells. The insertion is absent in other CoV-s of the same clade, including SARS-CoV1 that caused the 2003 outbreak. However, an analogous cleavage motif was present at S1/S2 of the Spike protein of the more distant Middle East Respiratory Syndrome coronavirus MERS-CoV. We show that a crucial third arginine at the left middle position, comprising a motif RRxR is required for furin recognition in vitro, while the general motif RxxR in common with MERS-CoV is not sufficient for cleavage. Further, we describe a surprising finding that the two serines at the edges of the insert SPRRAR downward arrowSV can be efficiently phosphorylated by proline-directed and basophilic protein kinases. Both phosphorylations switch off furin's ability to cleave the site. Although phospho-regulation of secreted proteins is still poorly understood, further studies, supported by a recent report of ten in vivo phosphorylated sites in the Spike protein of SARS-CoV2, could potentially uncover important novel regulatory mechanisms for SARS-CoV2.
|Amino Acid Motifs/genetics[MESH]
|Amino Acid Sequence[MESH]
|Betacoronavirus/*genetics[MESH]
|Furin/metabolism[MESH]
|Middle East Respiratory Syndrome Coronavirus/*genetics[MESH]