Comparisons between the Primary Structure of the Coat Proteins of Turnip Yellow Mosaic Virus and Eggplant Mosaic Virus

Dupin, A.; Collot, Daniel; Peter, R.; Witz, Jean‐François

doi:10.1099/0022-1317-66-12-2571

Cited by 9 publications

(2 citation statements)

References 26 publications

(34 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Tymoviruses lack strong RNA-protein interactions due to missing specific regions rich in basic residues in CP amino acid composition ( Dupin et al, 1985 ). As described above, during infection, Tymoviruses may produce two types of virions—one that contains a single viral genome (approximately 35% of their mass) as well as free “empty” protein shells, while some of those empty VLPs may pack small RNA molecules from their hosts ( Gibbs and Mackenzie, 1998 ).…”

Section: Resultsmentioning

confidence: 99%

Bacterial expression systems based on Tymovirus-like particles for the presentation of vaccine antigens

et al. 2023

View full text Add to dashboard Cite

Virus-like particles (VLPs) are virus-derived artificial nanostructures that resemble a native virus-stimulating immune system through highly repetitive surface structures. Improved safety profiles, flexibility in vaccine construction, and the ease of VLP production and purification have highlighted VLPs as attractive candidates for universal vaccine platform generation, although exploration of different types of expression systems for their development is needed. Here, we demonstrate the construction of several simple Escherichia coli expression systems for the generation of eggplant mosaic virus (EMV) VLP-derived vaccines. We used different principles of antigen incorporation, including direct fusion of EMV coat protein (CP) with major cat allergen Feld1, coexpression of antigen containing and unmodified (mosaic) EMV CPs, and two coexpression variants of EMV VLPs and antigen using synthetic zipper pair 18/17 (SYNZIP 18/17), and coiled-coil forming peptides E and K (Ecoil/Kcoil). Recombinant Fel d 1 chemically coupled to EMV VLPs was included as control experiments. All EMV-Feld1 variants were expressed in E. coli, formed Tymovirus-like VLPs, and were used for immunological evaluation in healthy mice. The immunogenicity of these newly developed vaccine candidates demonstrated high titers of Feld1-specific Ab production; however, a comparably high immune response against carrier EMV was also observed. Antibody avidity tests revealed very specific Ab production (more than 50% specificity) for four out of the five vaccine candidates. Native Feld1 recognition and subclass-specific antibody tests suggested that the EMV-SZ18/17-Feld1 complex and chemically coupled EMV-Feld1 vaccines may possess characteristics for further development.

show abstract

Section: Resultsmentioning

confidence: 99%

Bacterial expression systems based on Tymovirus-like particles for the presentation of vaccine antigens

et al. 2023

View full text Add to dashboard Cite

show abstract

“…of eggplant mosaic virus (another tymovirus) which presents 32% homology with the C.P. of TYMV [51]. Further comparisons of nt and amino acid sequences with other TYMV strains isolated in Australia (Gibbs et al, in preparation) should help in distinguishing conserved essential sequences from variable sequences or strain specific sequences.…”

Section: Discussionmentioning

confidence: 99%

Overlapping open reading frames revealed by complete nucleotide sequencing of turnip yellow mosaic virus genomic RNA

Morch

Boyer

Haenni

1988

Nucleic Acids Research

124

View full text Add to dashboard Cite

The complete nucleotide sequence of turnip yellow mosaic virus (TYMV) genomic RNA has been determined on a set of overlapping cDNA clones using a sequential sequencing strategy. The RNA is 6318 nucleotides long, excluding the cap structure. The genome organization deduced from the sequence confirms previous results of in vitro translation. A novel open reading frame (ORF) putatively encoding a Pro-rich and very basic 69K (K = kilodalton) protein is detected at the 5' end of the genome. It is initiated at the first AUG codon on the RNA and overlaps the major ORF that encodes the non structural 206K (previously referred to as 195K) protein of TYMV; its function is unknown. Several amino acid consensus sequences already described among plant and animal viruses are also found in the TYMV-encoded polypeptides. A comparison with other viruses whose RNA sequence is known leads to the conclusion that TYMV belongs to the "Sindbis-like" supergroup of viruses and could be related to Semliki forest virus.

show abstract

Tymoviruses

Hirth¹,

Givord²

1988

The Plant Viruses

View full text Add to dashboard Cite

Comparisons between the Primary Structure of the Coat Proteins of Turnip Yellow Mosaic Virus and Eggplant Mosaic Virus

Cited by 9 publications

References 26 publications

Bacterial expression systems based on Tymovirus-like particles for the presentation of vaccine antigens

Bacterial expression systems based on Tymovirus-like particles for the presentation of vaccine antigens

Overlapping open reading frames revealed by complete nucleotide sequencing of turnip yellow mosaic virus genomic RNA

Tymoviruses

Contact Info

Product

Resources

About