title: Potato virus Y-like particles as a new carrier for the presentation of foreign protein stretches.
abstract: Virus-like particle (VLP) technology represents a promising approach for the creation of efficient vaccines and materials for use in nanotechnological applications. For construction of a new carrier for foreign protein sequences, the coat protein (CP) gene from potato virus Y (PVY) was cloned and expressed in Escherichia coli cells. The PVY CP self-assembles into PVY-like particles, as demonstrated by electron microscopy analysis of purified VLP preparations. The PVY CP with an N-terminal insertion of a foreign epitope (preS1) or of a whole protein (rubredoxin) retains its ability to form filamentous particles, whereas adding a foreign sequence to the C-terminus of the PVY CP generates mostly unstructured protein aggregates. This new filamentous plant virus-derived VLP carrier accommodates a foreign protein sequence that is up to 71 amino acids in length on the VLP surface and can be produced in E. coli in preparative amounts. The PVY CP VLPs are stable in physiological conditions, but they are sensitive to EDTA, high salt, and extreme pH. The presence of the preS1 epitope decreases the stability of the chimeric PVY CP particles at elevated temperatures. Mice that are immunized with chimeric PVY CP particles carrying preS1 epitopes exhibit a strong anti-preS1 immune response, even in the absence of adjuvants.
authors.affiliation: Latvian Biomedical Research and Study Centre, Ratsupites 1, Riga LV-1067, Latvia. ievina_k@inbox.lv
authors.forename: Ieva
authors.initials: I
authors.lastname: Kalnciema
authors.forename: Dace
authors.initials: D
authors.lastname: Skrastina
authors.forename: Velta
authors.initials: V
authors.lastname: Ose
authors.forename: Paul
authors.initials: P
authors.lastname: Pumpens
authors.forename: Andris
authors.initials: A
authors.lastname: Zeltins
mesh_terms: D000818:Animals; D017951:Antigen Presentation; D001709:Biotechnology / Q000379:methods; D036022:Capsid Proteins / Q000235:genetics / Q000276:immunology / Q000378:metabolism*; D003001:Cloning, Molecular; D000939:Epitopes / Q000235:genetics / Q000276:immunology / Q000378:metabolism; D004926:Escherichia coli / Q000235:genetics* / Q000276:immunology / Q000378:metabolism; D005260:Female; D006510:Hepatitis B Antibodies / Q000097:blood; D006514:Hepatitis B Surface Antigens / Q000235:genetics / Q000276:immunology* / Q000378:metabolism; D006515:Hepatitis B virus / Q000235:genetics / Q000276:immunology / Q000378:metabolism; D007114:Immunization; D051379:Mice; D008807:Mice, Inbred BALB C; D017800:Potyvirus / Q000235:genetics*; D011498:Protein Precursors / Q000235:genetics / Q000276:immunology* / Q000378:metabolism; D011993:Recombinant Fusion Proteins / Q000235:genetics / Q000276:immunology / Q000378:metabolism; D058425:Vaccines, Virus-Like Particle / Q000276:immunology*; D014771:Virion / Q000235:genetics* / Q000276:immunology / Q000378:metabolism
chemical_list: D036022:Capsid Proteins; D000939:Epitopes; D006510:Hepatitis B Antibodies; D006514:Hepatitis B Surface Antigens; D011498:Protein Precursors; D011993:Recombinant Fusion Proteins; D058425:Vaccines, Virus-Like Particle; C050806:presurface protein 1, hepatitis B surface antigen; C090960:coat protein, Potato virus Y