Mosaic Qbeta coats as a new presentation model.
The new protein carrier was developed on the basis of recombinant RNA phage Qbeta capsid. C-terminal UGA extension of the short form of Qbeta coat, so-called A1 extension, served as a target for presentation of foreign peptides on the outer surface of mosaic Qbeta particles. In conditions of enhanced UGA suppression, the proportion of A1-extended to short coats in mosaic particles dropped from 48% to 14%, with an increase of the length of A1 extension. A model insertion, short preS1 epitope 31-DPAFR-35 of hepatitis B surface antigen, demonstrated superficial location on the mosaic Qbeta particles and ensured specific antigenicity and immunogenicity.
Biomedical Research and Study Centre, University of Latvia, Riga.
I
I
Vasiljeva
T
T
Kozlovska
I
I
Cielens
A
A
Strelnikova
A
A
Kazaks
V
V
Ose
P
P
Pumpens
D017908:Allolevivirus / Q000235:genetics* / Q000276:immunology / Q000648:ultrastructure; D000818:Animals; D002213:Capsid / Q000235:genetics* / Q000276:immunology; D036022:Capsid Proteins; D003001:Cloning, Molecular; D018388:Codon, Terminator; D005822:Genetic Vectors; D051379:Mice; D008807:Mice, Inbred BALB C; D019151:Peptide Library; D011993:Recombinant Fusion Proteins / Q000235:genetics / Q000276:immunology; D019065:Virus Assembly
D036022:Capsid Proteins; D018388:Codon, Terminator; D019151:Peptide Library; D011993:Recombinant Fusion Proteins; C043366:coat protein, Bacteriophage Qbeta