ArticleJournal of virology2005
Luxury at a cost? Recombinant mouse hepatitis viruses expressing the accessory hemagglutinin esterase protein display reduced fitness in vitro.
Article in Journal of virology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
34 citing papers in PubMed, 76 citations in OpenAlex.
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- SDAV, the Rat Coronavirus-How Much Do We Know about It in the Light of Potential Zoonoses.Viruses · 2021Review
- In silico investigation of critical binding pattern in SARS-CoV-2 spike protein with angiotensin-converting enzyme 2.Scientific reports · 2021Article
- Recent Progress in Torovirus Molecular Biology.Viruses · 2021Review
- Characterization of Localization and Export Signals of Bovine Torovirus Nucleocapsid Protein Responsible for Extensive Nuclear and Nucleolar Accumulation and Their Importance for Virus Growth.Journal of virology · 2021Article
- Physiologic RNA targets and refined sequence specificity of coronavirus EndoU.RNA (New York, N.Y.) · 2020Article
- Coronavirus hemagglutinin-esterase and spike proteins coevolve for functional balance and optimal virion avidity.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Point-of-Care Diagnostics of COVID-19: From Current Work to Future Perspectives.Sensors (Basel, Switzerland) · 2020Review
- Coronaviruses: An Updated Overview of Their Replication and Pathogenesis.Methods in molecular biology (Clifton, N.J.) · 2020Review
- Porcine Hemagglutinating Encephalomyelitis Virus: A Review.Frontiers in veterinary science · 2019Review
- Article
- Middle East Respiratory Coronavirus Accessory Protein 4a Inhibits PKR-Mediated Antiviral Stress Responses.PLoS pathogens · 2016Article
- The contribution of the cytoplasmic retrieval signal of severe acute respiratory syndrome coronavirus to intracellular accumulation of S proteins and incorporation of S protein into virus-like particles.The Journal of general virology · 2016Article
- Review
- Coronaviruses: an overview of their replication and pathogenesis.Methods in molecular biology (Clifton, N.J.) · 2015Review
- Negatively charged residues in the endodomain are critical for specific assembly of spike protein into murine coronavirus.Virology · 2013Article
- Porcine epidemic diarrhoea virus: a comprehensive review of molecular epidemiology, diagnosis, and vaccines.Virus genes · 2012Review
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Group 2 coronaviruses encode an accessory envelope glycoprotein species, the hemagglutinin esterase (HE), which possesses sialate-O-acetylesterase activity and which, presumably, promotes virus spread and entry in vivo by facilitating reversible virion attachment to O-acetylated sialic acids. While HE may provide a strong selective advantage during natural infection, many laboratory strains of mouse hepatitis virus (MHV) fail to produce the protein. Apparently, their HE genes were inactivated during cell culture adaptation. For this report, we have studied the molecular basis of this phenomenon. By using targeted RNA recombination, we generated isogenic recombinant MHVs which differ exclusively in their expression of HE and produce either the wild-type protein (HE+), an enzymatically inactive HE protein (HE0), or no HE at all. HE expression or the lack thereof did not lead to gross differences in in vitro growth properties. Yet the expression of HE was rapidly lost during serial cell culture passaging. Competition experiments with mixed infections revealed that this was not due to the enzymatic activity: MHVs expressing HE+ or HE0 propagated with equal efficiencies. During the propagation of recombinant MHV-HE+, two types of spontaneous mutants accumulated. One produced an anchorless HE, while the other had a Gly-to-Trp substitution at the predicted C-terminal residue of the HE signal peptide. Neither mutant incorporated HE into virion particles, suggesting that wild-type HE reduces the in vitro propagation efficiency, either at the assembly stage or at a postassembly level. Our findings demonstrate that the expression of "luxury" proteins may come at a fitness penalty. Apparently, under natural conditions the costs of maintaining HE are outweighed by the benefits.
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