Why the study?
The study was conducted to determine the prevalence, types of RSV, and sequence variability of the G and F genes in Hungary between 2017 and 2023.
Circulating RSV strains in Hungary from 2017 to 2023 showed sequence variations but no mutations that would reduce the efficacy of nirsevimab.
Our study determined the prevalence, types of RSV, and sequence variability of the G and F genes in Hungary between 2017 and 2023. During the study, 1828 respiratory samples were collected from hospitalised pediatric patients. We confirmed the presence of RSV A in 12.74%, RSV B in 13.85%, and their simultaneous presence in 0.27%. The highest RSV positivity was observed in the 2018-2019 season, while the lowest was in the 2017-2018 season. Following the SARS-CoV-2 pandemic, the RSV season has an earlier onset and longer duration than it did previously; however, an earlier onset was already detected in 2018. All RSV A isolates are classified into the A.D., while RSV B into the B.D. clades. The entire ectodomain of G protein showed a high sequence diversity, higher than in the case of B.D. strains. Mutations at position 276, adjacent to the palivizumab binding site of the F protein, could be detected. At the same time, neither K272E/N nor any other mutation is present in the palivizumab binding region in our strains. Several mutations in the nirsevimab binding region could be detected in our strains; however, none of these mutations, which would affect nirsevimab activity, were found in our isolates. • We studied circulating RSV strains and their seasonality in Hungary from 2017 to 2023 in children under 18. • The SARS-CoV-2 pandemic's restrictions altered the seasonal patterns of respiratory infections. • Our isolates exhibit several sequence variations in the G and F proteins and can be classified into A.D. and B.D. clades. • RSV A strains belonging to the 2019–2020 clade exhibit a rare amino acid substitution pattern in the HRV1 and HRV2 region, like two German isolates in GenBank. • We found no N208D and I64M combined with K65R or any other mutations that reduce nirsevimab activity.
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Juhász et al. (2026) studied this question.
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