ArticleVirology2013
Role of the vaccinia virus O3 protein in cell entry can be fulfilled by its Sequence flexible transmembrane domain.
Article in Virology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 11 citations in OpenAlex.
- Insights into Genomic Dynamics and Plasticity in the Monkeypox Virus from the 2022 Outbreak.International journal of molecular sciences · 2026Article
- Poxvirus structural biology for application to vaccine design.Trends in immunology · 2025Review
- Structure-Function Analysis of Two Interacting Vaccinia Proteins That Are Critical for Viral Morphogenesis: L2 and A30.5.Journal of virology · 2022Article
- Insights into the Organization of the Poxvirus Multicomponent Entry-Fusion Complex from Proximity Analyses in Living Infected Cells.Journal of virology · 2021Article
- Loss of the vaccinia virus 35-amino acid hydrophobic O3 protein is partially compensated by mutations in the transmembrane domains of other entry proteins.Journal of virology · 2021Article
- Investigation of amino acid specificity in the CydX small protein shows sequence plasticity at the functional level.PloS one · 2018Article
- Membrane fusion during poxvirus entry.Seminars in cell & developmental biology · 2016Review
- Review
- De novo selection of oncogenes.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Viral miniproteins.Annual review of microbiology · 2014Review
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The vaccinia virus O3 protein, a component of the entry-fusion complex, is encoded by all chordopoxviruses. We constructed truncation mutants and demonstrated that the transmembrane domain, which comprises two-thirds of this 35 amino acid protein, is necessary and sufficient for interaction with the entry-fusion complex and function in cell entry. Nevertheless, neither single amino acid substitutions nor alanine scanning mutagenesis revealed essential amino acids within the transmembrane domain. Moreover, replication-competent mutant viruses were generated by randomization of 10 amino acids of the transmembrane domain. Of eight unique viruses, two contained only two amino acids in common with wild type and the remainder contained one or none within the randomized sequence. Although these mutant viruses formed normal size plaques, the entry-fusion complex did not co-purify with the mutant O3 proteins suggesting a less stable interaction. Thus, despite low specific sequence requirements, the transmembrane domain is sufficient for function in entry.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.