ArticlePloS one2013
Identifying SARS-CoV membrane protein amino acid residues linked to virus-like particle assembly.
Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers, 1 of them a synthesis that pooled it.
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Who cites it
36 citing papers in PubMed, 1 synthesis or guideline pooled it, 57 citations in OpenAlex.
- Review: A systematic review of virus-like particles of coronavirus: Assembly, generation, chimerism and their application in basic research and in the clinic.International journal of biological macromolecules · 2022Pooled it
- Beyond assembly: functions of the coronavirus M protein.Virology journal · 2026Review
- The structure and function of membrane protein in coronavirus infection and its applications in the development of vaccines and therapeutic drugs.Frontiers in microbiology · 2026Review
- Review
- Sequential glycosylations at the multibasic cleavage site of SARS-CoV-2 spike protein regulate viral activity.Nature communications · 2024Article
- Multiple Lines of Evidence Support 199 SARS-CoV-2 Positively Selected Amino Acid Sites.International journal of molecular sciences · 2024Article
- Structural proteins of human coronaviruses: what makes them different?Frontiers in cellular and infection microbiology · 2024Review
- Emerging trends in point-of-care biosensing strategies for molecular architectures and antibodies of SARS-CoV-2.Biosensors & bioelectronics: X · 2023Review
- Perturbation of the host cell CaCell death & disease · 2023Article
- A review on structural, non-structural, and accessory proteins of SARS-CoV-2: Highlighting drug target sites.Immunobiology · 2023Review
- Non-uniform aspects of the SARS-CoV-2 intraspecies evolution reopen question of its origin.International journal of biological macromolecules · 2022Article
- Three-Dimensional Visualization of Viral Structure, Entry, and Replication Underlying the Spread of SARS-CoV-2.Chemical reviews · 2022Review
- Evolution of the SARS-CoV-2 proteome in three dimensions (3D) during the first 6 months of the COVID-19 pandemic.Proteins · 2022Article
- SARS-CoV-2 Membrane Protein: From Genomic Data to Structural New Insights.International journal of molecular sciences · 2022Article
- Structural biology of SARS-CoV-2: open the door for novel therapies.Signal transduction and targeted therapy · 2022Review
- The Complexity of SARS-CoV-2 Infection and the COVID-19 Pandemic.Frontiers in microbiology · 2022Review
- Molecular interactions of the M and E integral membrane proteins of SARS-CoV-2.Faraday discussions · 2021Article
- Differential mutation profile of SARS-CoV-2 proteins across deceased and asymptomatic patients.Chemico-biological interactions · 2021Article
- Therapeutic targets and interventional strategies in COVID-19: mechanisms and clinical studies.Signal transduction and targeted therapy · 2021Review
- Sequence and structural analysis of COVID-19 E and M proteins with MERS virus E and M proteins-A comparative study.Biochemistry and biophysics reports · 2021Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Severe acute respiratory syndrome coronavirus (SARS-CoV) membrane (M) proteins are capable of self-assembly and release in the form of membrane-enveloped vesicles, and of forming virus-like particles (VLPs) when coexpressed with SARS-CoV nucleocapsid (N) protein. According to previous deletion analyses, M self-assembly involves multiple M sequence regions. To identify important M amino acid residues for VLP assembly, we coexpressed N with multiple M mutants containing substitution mutations at the amino-terminal ectodomain, carboxyl-terminal endodomain, or transmembrane segments. Our results indicate that a dileucine motif in the endodomain tail (218LL219) is required for efficient N packaging into VLPs. Results from cross-linking VLP analyses suggest that the cysteine residues 63, 85 and 158 are not in close proximity to the M dimer interface. We noted a significant reduction in M secretion due to serine replacement for C158, but not for C63 or C85. Further analysis suggests that C158 is involved in M-N interaction. In addition to mutations of the highly conserved 107-SWWSFNPE-114 motif, substitutions at codons W19, W57, P58, W91, Y94 or F95 all resulted in significantly reduced VLP yields, largely due to defective M secretion. VLP production was not significantly affected by a tryptophan replacement of Y94 or F95 or a phenylalanine replacement of W19, W57 or W91. Combined, these results indicate the involvement of specific M amino acids during SARS-CoV virus assembly, and suggest that aromatic residue retention at specific positions is critical for M function in terms of directing virus assembly.
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