AVM

Mutation site	N331Q/N343Q
Virus	SARS-CoV-2
Mutation level	Amino acid level
Gene/protein/region type	S
Gene ID	43740568
Country	-
Mutation type	nonsynonymous mutation
Genotype/subtype/clade	-
Sample	cell line
Variants	-
Viral reference sequence	NC_045512.2
Drug/antibody/vaccine	-
Transmissibility	hinder
Transmission mechanism	More importantly, based on qualitative and quantitative virology research methods, we show that the mutation of RBD N-glycosites interfered with SARS-CoV-2 internalization rather than attachment potentially by decreasing RBD binding to the receptors. Also
Pathogenicity	-
Pathogenicity mechanism	-
Immune escape mutation	-
Immune escape mechanism	-
RT-PCR primers probes	-

Protein name	Spike glycoprotein
Uniprot protein ID	P0DTC2
Protein length	1273 amino acids
Protein description	Spike protein is one of the structural proteins of SARS-CoV-2. The monomeric protein consists of one large ectodomain, a single-pass transmembrane anchor, and a short intracellular tail at C-terminus. It encompasses 22 glycosylation sites. S protein cleaves into two subunits namely S1 and S2 following receptor recognition. Receptor Binding Domain (RBD) in S1 subunit plays a major role in ACE2 receptor binding.

Pubmed ID	34592572
Clinical information	No
Disease	-
Published year	2021
Journal	Biochem Biophys Res Commun
Title	SARS-CoV-2 spike protein receptor-binding domain N-glycans facilitate viral internalization in respiratory epithelial cells
Author	Luping Zheng, Yingxin Ma, Minghai Chen, Guoqiang Wu, Chuang Yan
Evidence	Notably, the binding between WT S1 and recombinant ACE2 was highly stable; however, the double de-glycosylation (N331Q + N343Q) drastically reduced the binding(Fig. 1B and C). The respective single deletions also reduced the binding, albeit mildly, compared to the N331Q + N343Q (Fig. 1B and C).