@goerzerlab.bsky.social
Virology lab studying various aspects of entry glycoproteins of the human cytomegalovirus, part of the Center for Virology at the Medical University Vienna
Reposted
after Bacmid transfection revealed compensatory second-site mutations, mainly in domain V, reverting this atypical phenotype and rescuing the infection capability. We suggest an important interaction between domains III and V during the fusion process.
January 9, 2025 at 4:09 PM
after Bacmid transfection revealed compensatory second-site mutations, mainly in domain V, reverting this atypical phenotype and rescuing the infection capability. We suggest an important interaction between domains III and V during the fusion process.
Reposted
Madlen Mollik from @goerzerlab.bsky.social pubmed.ncbi.nlm.nih.gov/39315800/
In this paper, we characterized four mutations in domain III of HCMV gB, of which one depicted an atypical phenotype in fibroblasts upon long-term culturing. Sequencing of reconstituted viruses at various time points
In this paper, we characterized four mutations in domain III of HCMV gB, of which one depicted an atypical phenotype in fibroblasts upon long-term culturing. Sequencing of reconstituted viruses at various time points
January 9, 2025 at 4:09 PM
Madlen Mollik from @goerzerlab.bsky.social pubmed.ncbi.nlm.nih.gov/39315800/
In this paper, we characterized four mutations in domain III of HCMV gB, of which one depicted an atypical phenotype in fibroblasts upon long-term culturing. Sequencing of reconstituted viruses at various time points
In this paper, we characterized four mutations in domain III of HCMV gB, of which one depicted an atypical phenotype in fibroblasts upon long-term culturing. Sequencing of reconstituted viruses at various time points