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Mosaic Qβ coats as a new presentation model
Author(s) -
Vasiljeva Inta,
Kozlovska Tatjana,
Cielens Indulis,
Strelnikova Anna,
Kazaks Andris,
Ose Velta,
Pumpens Paul
Publication year - 1998
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(98)00716-9
Subject(s) - capsid , virology , antigenicity , epitope , immunogenicity , biology , cryo electron microscopy , recombinant dna , chemistry , antigen , virus , biophysics , genetics , gene
The new protein carrier was developed on the basis of recombinant RNA phage Qβ capsid. C‐terminal UGA extension of the short form of Qβ coat, so‐called A1 extension, served as a target for presentation of foreign peptides on the outer surface of mosaic Qβ 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 Qβ particles and ensured specific antigenicity and immunogenicity.