SARS-CoV-2 Mutation Detail Information

Virus Mutation SARS-CoV-2 Mutation G502M


Basic Characteristics of Mutations
Mutation Site G502M
Mutation Site Sentence Among low-frequency mutations within or near RBS, we selected seven amino acid mutations, S443N, G447H, F456D, N487G, Y489S, T500D, and G502M, as RBD mutants for the initial antibody screening (Fig. 1a, b).
Mutation Level Amino acid level
Mutation Type Nonsynonymous substitution
Gene/Protein/Region RBD
Standardized Encoding Gene S  
Genotype/Subtype -
Viral Reference EMDB: EMD-2145241
Functional Impact and Mechanisms
Disease Cell line    
Immune -
Target Gene ACE2   
Clinical and Epidemiological Correlations
Clinical Information -
Treatment -
Location -
Literature Information
PMID 37452031
Title Structural delineation and computational design of SARS-CoV-2-neutralizing antibodies against Omicron subvariants
Author Moriyama S,Anraku Y,Taminishi S,Adachi Y,Kuroda D,Kita S,Higuchi Y,Kirita Y,Kotaki R,Tonouchi K,Yumoto K,Suzuki T,Someya T,Fukuhara H,Kuroda Y,Yamamoto T,Onodera T,Fukushi S,Maeda K,Nakamura-Uchiyama F,Hashiguchi T,Hoshino A,Maenaka K,Takahashi Y
Journal Nature communications
Journal Info 2023 Jul 14;14(1):4198
Abstract SARS-CoV-2 Omicron subvariants have evolved to evade receptor-binding site (RBS) antibodies that exist in diverse individuals as public antibody clones. We rationally selected RBS antibodies resilient to mutations in emerging Omicron subvariants. Y489 was identified as a site of virus vulnerability and a common footprint of broadly neutralizing antibodies against the subvariants. Multiple Y489-binding antibodies were encoded by public clonotypes and additionally recognized F486, potentially accounting for the emergence of Omicron subvariants harboring the F486V mutation. However, a subclass of antibodies broadly neutralized BA.4/BA.5 variants via hydrophobic binding sites of rare clonotypes along with high mutation-resilience under escape mutation screening. A computationally designed antibody based on one of the Y489-binding antibodies, NIV-10/FD03, was able to bind XBB with any 486 mutation and neutralized XBB.1.5. The structural basis for the mutation-resilience of this Y489-binding antibody group may provide important insights into the design of therapeutics resistant to viral escape.
Sequence Data PRJNA970973;EMD-33821;EMD-33822 (PDB 7YH7);EMD-33820 (PDB 7YH6);EMD-33824;EMD-33825;EMD-33826;EMD-33823;PDB 8HES;EMD-34741 (PDB 8HGL);EMD-34732 (PDB 8HGM);EMD-33828;EMD-33829;EMD-33830
Mutation Information
Note
Basic Characteristics of Mutations
  • Mutation Site: The specific location in a gene or protein sequence where a change occurs.
  • Mutation Level: The level at which a mutation occurs, including the nucleotide or amino acid level.
  • Mutation Type: The nature of the mutation, such as missense mutation, nonsense mutation, synonymous mutation, etc.
  • Gene/Protein/Region: Refers to the specific region of the virus where the mutation occurs. Including viral genes, viral proteins, or a specific viral genome region. If the article does not specifically indicate the relationship between the mutation and its correspondence, the main
  • Gene/Protein/Region studied in the article is marked.
  • Genotype/Subtype: Refers to the viral genotype or subtype where the mutation occurs. If the article does not specifically indicate the relationship between the mutation and its correspondence, the main Genotype/Subtype studied in the article is marked.
  • Viral Reference: Refers to the standard virus strain used to compare and analyze viral sequences.
Functional Impact and Mechanisms
  • Disease: An abnormal physiological state with specific symptoms and signs caused by viral infection.
  • Immune: The article focuses on the study of mutations and immune.
  • Target Gene: Host genes that viral mutations may affect.
Clinical and Epidemiological Correlations
  • Clinical Information: The study is a clinical or epidemiological study and provides basic information about the population.
  • Treatment: The study mentioned a certain treatment method, such as drug resistance caused by mutations. If the study does not specifically indicate the relationship between mutations and their correspondence treatment, the main treatment studied in the article is marked.
  • Location: The source of the research data.
Literature Information
  • Sequence Data: The study provides the data accession number.