ArticleThe Journal of biological chemistry2014
Site-specific S-acylation of influenza virus hemagglutinin: the location of the acylation site relative to the membrane border is the decisive factor for attachment of stearate.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 50 citations in OpenAlex.
- Positive Regulation of Cellular Proteins by Influenza Virus for Productive Infection.International journal of molecular sciences · 2025Review
- Cell Labeling with 15-YNE Is Useful for Tracking Protein Palmitoylation and Metabolic Lipid Flux in the Same Sample.Molecules (Basel, Switzerland) · 2025Article
- Exploring protein lipidation by mass spectrometry-based proteomics.Journal of biochemistry · 2024Review
- Amino acid and protein specificity of protein fatty acylation inProceedings of the National Academy of Sciences of the United States of America · 2024Article
- Molecular Mechanisms behind Conformational Transitions of the Influenza Virus Hemagglutinin Membrane Anchor.The journal of physical chemistry. B · 2023Article
- The role of an amphiphilic helix and transmembrane region in the efficient acylation of the M2 protein from influenza virus.Scientific reports · 2023Article
- Cysteine residues in signal transduction and its relevance in pancreatic beta cells.Frontiers in endocrinology · 2023Review
- Molecular Dynamics of DHHC20 Acyltransferase Suggests Principles of Lipid and Protein Substrate Selectivity.International journal of molecular sciences · 2022Article
- Protein Lipidation Types: Current Strategies for Enrichment and Characterization.International journal of molecular sciences · 2022Review
- Protein Palmitoylation Modification During Viral Infection and Detection Methods of Palmitoylated Proteins.Frontiers in cellular and infection microbiology · 2022Review
- Stearic acid blunts growth-factor signaling via oleoylation of GNAI proteins.Nature communications · 2021Article
- Acyl-CoA thioesterase activity of peroxisomal ABC protein ABCD1 is required for the transport of very long-chain acyl-CoA into peroxisomes.Scientific reports · 2021Article
- Regulation of Dynamic Protein S-Acylation.Frontiers in molecular biosciences · 2021Review
- Structure and Mechanism of DHHC Protein Acyltransferases.Journal of molecular biology · 2020Review
- Review
- The inducible amphisome isolates viral hemagglutinin and defends against influenza A virus infection.Nature communications · 2020Article
- Cholesterol Binding to the Transmembrane Region of a Group 2 Hemagglutinin (HA) of Influenza Virus Is Essential for Virus Replication, Affecting both Virus Assembly and HA Fusion Activity.Journal of virology · 2019Article
- Orchestration of protein acetylation as a toggle for cellular defense and virus replication.Nature communications · 2018Article
- Mass-Tag Labeling Using Acyl-PEG Exchange for the Determination of Endogenous Protein S-Fatty Acylation.Current protocols in protein science · 2017Article
- Molecular basis of fatty acid selectivity in the zDHHC family of S-acyltransferases revealed by click chemistry.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
S-Acylation of hemagglutinin (HA), the main glycoprotein of influenza viruses, is an essential modification required for virus replication. Using mass spectrometry, we have previously demonstrated specific attachment of acyl chains to individual acylation sites. Whereas the two cysteines in the cytoplasmic tail of HA contain only palmitate, stearate is exclusively attached to a cysteine positioned at the end of the transmembrane region (TMR). Here we analyzed recombinant viruses containing HA with exchange of conserved amino acids adjacent to acylation sites or with a TMR cysteine shifted to a cytoplasmic location to identify the molecular signal that determines preferential attachment of stearate. We first developed a new protocol for sample preparation that requires less material and might thus also be suitable to analyze cellular proteins. We observed cell type-specific differences in the fatty acid pattern of HA: more stearate was attached if human viruses were grown in mammalian compared with avian cells. No underacylated peptides were detected in the mass spectra, and even mutations that prevented generation of infectious virus particles did not abolish acylation of expressed HA as demonstrated by metabolic labeling experiments with [(3)H]palmitate. Exchange of conserved amino acids in the vicinity of an acylation site had a moderate effect on the stearate content. In contrast, shifting the TMR cysteine to a cytoplasmic location virtually eliminated attachment of stearate. Thus, the location of an acylation site relative to the transmembrane span is the main signal for stearate attachment, but the sequence context and the cell type modulate the fatty acid pattern.
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