About: A single amino acid substitution (R441A) in the receptor-binding domain of SARS coronavirus spike protein disrupts the antigenic structure and binding activity

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About: A single amino acid substitution (R441A) in the receptor-binding domain of SARS coronavirus spike protein disrupts the antigenic structure and binding activity Goto Sponge NotDistinct Permalink

An Entity of Type : schema:ScholarlyArticle, within Data Space : wasabi.inria.fr associated with source document(s)

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type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	A single amino acid substitution (R441A) in the receptor-binding domain of SARS coronavirus spike protein disrupts the antigenic structure and binding activity
Creator	He, Yuxian Jiang, Shibo Li, Jingjing
Source	Elsevier; Medline; PMC
abstract	Abstract The spike (S) protein of severe acute respiratory syndrome coronavirus (SARS-CoV) has two major functions: interacting with the receptor to mediate virus entry and inducing protective immunity. Coincidently, the receptor-binding domain (RBD, residues 318–510) of SAR-CoV S protein is a major antigenic site to induce neutralizing antibodies. Here, we used RBD-Fc, a fusion protein containing the RBD and human IgG1 Fc, as a model in the studies and found that a single amino acid substitution in the RBD (R441A) could abolish the immunogenicity of RBD to induce neutralizing antibodies in immunized mice and rabbits. With a panel of anti-RBD mAbs as probes, we observed that R441A substitution was able to disrupt the majority of neutralizing epitopes in the RBD, suggesting that this residue is critical for the antigenic structure responsible for inducing protective immune responses. We also demonstrated that the RBD-Fc bearing R441A mutation could not bind to soluble and cell-associated angiotensin-converting enzyme 2 (ACE2), the functional receptor for SARS-CoV and failed to block S protein-mediated pseudovirus entry, indicating that this point mutation also disrupted the receptor-binding motif (RBM) in the RBD. Taken together, these data provide direct evidence to show that a single amino acid residue at key position in the RBD can determine the major function of SARS-CoV S protein and imply for designing SARS vaccines and therapeutics.
has issue date	2006-05-26(xsd:dateTime)
bibo:doi	10.1016/j.bbrc.2006.03.139
bibo:pmid	16615996
has license	els-covid
sha1sum (hex)	6d50bf341565861b08e412d7d8a13619c119334c
schema:url	https://doi.org/10.1016/j.bbrc.2006.03.139
resource representing a document's title	A single amino acid substitution (R441A) in the receptor-binding domain of SARS coronavirus spike protein disrupts the antigenic structure and binding activity
has PubMed Central identifier	PMC7092835
has PubMed identifier	16615996
schema:publication	Biochemical and Biophysical Research Communications
resource representing a document's body	covid:6d50bf341565861b08e412d7d8a13619c119334c#body_text
is schema:about of	named entity 'AMINO ACID SUBSTITUTION' named entity 'PROTEIN ' named entity 'induce' named entity 'key' named entity 'neutralizing antibodies' named entity 'protein' named entity 'position' named entity 'SINGLE' named entity 'DETERMINE' named entity 'PSEUDOVIRUS' named entity 'BINDING' named entity 'MEDIATE' named entity 'AMINO ACID SUBSTITUTION' named entity 'FUNCTIONS' named entity 'FUNCTION' named entity 'VACCINES' named entity 'RABBITS' named entity 'STRUCTURE' named entity 'MAJOR' named entity 'INDUCING' named entity 'SITE' named entity 'DISRUPT' named entity 'MOTIF' named entity 'SARS CORONAVIRUS' named entity 'SUBSTITUTION' named entity 'POSITION' named entity 'BEARING' named entity 'FAILED' named entity 'DATA' named entity 'RBD' named entity 'PROTEIN ' named entity 'TAKEN' named entity 'SARS-COV' named entity 'STUDIES' named entity 'CRITICAL' named entity 'IGG1' named entity 'PANEL' named entity 'PROTECTIVE IMMUNITY' named entity 'SPIKE PROTEIN' named entity 'DOMAIN' named entity 'DISRUPTED' named entity 'SINGLE' named entity 'NEUTRALIZING ANTIBODIES' named entity 'HERE' named entity 'FUSION PROTEIN' named entity 'ENTRY' named entity 'RECEPTOR' named entity 'BINDING ACTIVITY' named entity 'S PROTEIN' named entity 'IS A' named entity 'HUMAN' named entity 'IMMUNOGENICITY' named entity 'BINDING' named entity 'USED' named entity 'ASSOCIATED' named entity 'DOMAIN' named entity 'THESE' named entity 'STRUCTURE' named entity 'THERAPEUTICS' named entity 'FOUND' named entity '28S' named entity 'DISRUPTS' named entity 'SPIKE' named entity 'IMMUNIZED' named entity 'SEVERE ACUTE RESPIRATORY SYNDROME CORONAVIRUS' named entity 'OBSERVED' named entity 'AMINO ACID RESIDUE' named entity '510' named entity 'IMMUNE RESPONSES' named entity 'MEDIATED' named entity 'INDUCE' named entity 'INTERACTING' named entity 'MUTATION' named entity 'FUNCTIONAL' named entity 'RESPONSIBLE' named entity 'PROBES' named entity 'A MAJOR' named entity 'SAR' named entity 'EPITOPES'

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