For each diagnostic antibody evaluated, the researchers documented which mutations to the N protein affected antibody recognition. From this information, they created an ‘escape mutation profile’ for each antibody, which lists the specific mutations to the N protein that have an effect on the antibody’s ability to bind to its target. While several diagnostic antibodies recognized the same region of the N protein, the researchers found that each antibody had a unique escape mutation profile. As SARS-CoV-2 continues to develop mutations, this data can be used to flag specific antibodies whose diagnostic performance may need to be re-assessed. “Based on our findings, none of the major past and present SARS-CoV-2 variants of concern contain N protein mutations that would affect recognition by antibodies used in current rapid antigen tests,” said first study author Filipp Frank, Ph.D., an assistant professor in the department of biochemistry at Emory University, Atlanta. “Further, this data could inform test design by identifying which diagnostic antibodies should be paired to identify the maximum amount of potential N protein variations.”
“Accurate and efficient identification of infected individuals remains a critically important strategy for Covid-19 mitigation, and our study provides information about future SARS-CoV-2 mutations that may interfere with detection,” said senior study author Eric Ortlund, Ph.D., a professor in the department of biochemistry at Emory University. “The results outlined here can allow us to quickly adapt to the virus as new variants continue to emerge, representing an immediate clinical and public health impact.”
While many variants of concern contain multiple mutations to the N protein, the study authors note that their method does not evaluate how multiple mutations could affect diagnostic antibody recognition, representing a limitation of the study.
Source: National Institutes of Health
Source: Healthcare in Europe
