Discussion: With the T478I mutation, moderate resistance to neutralization by two monoclonal antibodies and convalescent sera from two COVID-19 patients has been documented.
Identification of SARS-CoV-2 spike mutations that attenuate monoclonal and serum antibody neutralization.
Result: Sera 13 and 35 also did not efficiently neutralize S477G, L441R, and T478I.
Result: Substitution L452R conferred resistance to SARS2-01, SARS2-02, and SARS2-32; S477N, S477G, and S477R were each highly resistant to SARS2-07, SARS2-16, and SARS2-19, and S477N and S477G result in a degree of resistance across the entire panel of antibodies; and T478I yielded resistance to SARS2-16 and SARS2-19.
Result: The penetrance of the remaining substitutions among clinical isolates is relatively low, with G446V, T478I, E484K,
Pan-India novel coronavirus SARS-CoV-2 genomics and global diversity analysis in spike protein.
Introduction: To assess the neutralization breadth of RBD-NP-elicited Abs, we evaluated serum neutralizing activity against a panel of pseudotyped viruses comprising wild-type (D614G) SARS-CoV-2 S and nine single-residue SARS-CoV-2 RBD mutants detected in clinical isolates (G446S, Y453F, L455F, T478I, E484A/K, F486L, S494P, and N501Y) as well as the B.1.1.7 (H69-V70 deletion, Y144 deletion, N501Y, A570D, P681H, T716I, PMID: 33908339
2021
Epidemiology and infection
Abstract: Cluster mutations namely N501Y (45%), E484K (30%), N439K (16%), K417N (6%) and T478I (3%) at spike protein have increased during January to February 2021.
Result: However, during the second wave starting from October 2020 substitution point mutations E780Q, K417N, T478I, N501Y, E484K, N439K, V1176F, S477N and A222V became common at spike protein in the isolates in Japan.
Table: T478I<
Vaccine-escape and fast-growing mutations in the United Kingdom, the United States, Singapore, Spain, India, and other COVID-19-devastated countries.
Introduction: A similar change at position 478 (T478I) was previously selected in vitro and shown to exhibit reduced neutralization by monoclonal antibodies and human convalescent sera.
Receptor binding, immune escape, and protein stability direct the natural selection of SARS-CoV-2 variants.
PMID: 34543625
2021
The Journal of biological chemistry
Result: Three of the 8 mutants, Y453F, T478I and S494P, did not show significant difference in their binding interaction with ACE2, with Kd and DeltaH values similar to the wild-type protein (Table 3).
Figure: Panels A-I show the data for the wild-type
Figure: The single mutants of RBD used in this study were K417N, N439K, Y453F, S477N, T478I, E484K, S494P and N501Y (Alpha variant).
Discussion: 7A), and hence mutations T478I and S494P do not bring any change to the binding affinity.
Mutations of SARS-CoV-2 RBD May Alter Its Molecular Structure to Improve Its Infection Efficiency.
Discussion: For instance, N439K, L452R, T478I, and E484D mutations on RBM have significant free energy changes, and they constitute approximately 58% of all mutations on RBD.
SARS_CoV_2 mutation literature information.
PMID: 
2022
International immunopharmacology
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