SARS-CoV-2 Mutation Detail Information

Virus Mutation SARS-CoV-2 Mutation K679N


Basic Characteristics of Mutations
Mutation Site K679N
Mutation Site Sentence Further, the average binding energy of the S1/S2 cleavage site with HAT was -308.9 kcal/mol for BA.1 H681P mutation, which is lower and stronger compared with that of the BA.1 K679N mutation with -279.6 kcal/mol (P < 0.05) (Supplemental Table 3).
Mutation Level Amino acid level
Mutation Type Nonsynonymous substitution
Gene/Protein/Region
Standardized Encoding Gene
Genotype/Subtype BA.1
Viral Reference -
Functional Impact and Mechanisms
Disease COVID-19    
Immune -
Target Gene -
Clinical and Epidemiological Correlations
Clinical Information -
Treatment HAT
Location Sichuan(China)
Literature Information
PMID 39286971
Title SARS-CoV-2 Delta and Omicron variants resist spike cleavage by human airway trypsin-like protease
Author Ren W,Hong W,Yang J,Zou J,Chen L,Zhou Y,Lei H,Alu A,Que H,Gong Y,Bi Z,He C,Fu M,Peng D,Yang Y,Yu W,Tang C,Huang Q,Yang M,Li B,Li J,Wang J,Ma X,Hu H,Cheng W,Dong H,Lei J,Chen L,Zhou X,Li J,Wang W,Lu G,Shen G,Yang L,Yang J,Wang Z,Jia G,Su Z,Shao B,Miao H,Yiu-Nam Lau J,Wei Y,Zhang K,Dai L,Lu S,Wei X
Journal The Journal of clinical investigation
Journal Info 2024 Sep 17;134(18):e174304
Abstract Soluble host factors in the upper respiratory tract can serve as the first line of defense against SARS-CoV-2 infection. In this study, we described the identification and function of a human airway trypsin-like protease (HAT), capable of reducing the infectivity of ancestral SARS-CoV-2. Further, in mouse models, HAT analogue expression was upregulated by SARS-CoV-2 infection. The antiviral activity of HAT functioned through the cleavage of the SARS-CoV-2 spike glycoprotein at R682. This cleavage resulted in inhibition of the attachment of ancestral spike proteins to host cells, which inhibited the cell-cell membrane fusion process. Importantly, exogenous addition of HAT notably reduced the infectivity of ancestral SARS-CoV-2 in vivo. However, HAT was ineffective against the Delta variant and most circulating Omicron variants, including the BQ.1.1 and XBB.1.5 subvariants. We demonstrate that the P681R mutation in Delta and P681H mutation in the Omicron variants, adjacent to the R682 cleavage site, contributed to HAT resistance. Our study reports what we believe to be a novel soluble defense factor against SARS-CoV-2 and resistance of its actions in the Delta and Omicron variants.
Sequence Data -
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.