OmpA—FMDV VP1 fusion proteins: production, cell surface exposure and immune responses to the major antigenic domain of foot-and-mouth disease virus

• Published in: Vaccine Vol. 12; no. 6; pp. 492 - 498
• Main Authors: Ruppert, Andreas, Arnold, Norbert, Hobom, Gerd
• Format: Journal Article
• Language: English
• Published: Oxford Elsevier Ltd 01.05.1994; Elsevier
• Subjects: Amino Acid Sequence; Animals; Antigens, Viral - immunology; Aphthovirus - immunology; Bacterial Outer Membrane Proteins - analysis; Bacterial Outer Membrane Proteins - genetics; Bacterial Outer Membrane Proteins - immunology; Base Sequence; Biological and medical sciences; Capsid - analysis; Capsid - genetics; Capsid - immunology; Capsid Proteins; cell surface exposure; Escherichia coli; FMDV VP1 fusion proteins; foot-and-mouth disease virus; Fundamental and applied biological sciences. Psychology; immune responses; Immunization; major antigenic domain; Microbiology; Molecular Sequence Data; OmpA; Rabbits; Recombinant Fusion Proteins - biosynthesis; Recombinant Fusion Proteins - immunology; Shigella dysenteriae; Vaccines, antisera, therapeutical immunoglobulins and monoclonal antibodies; Virology; FMDV VP1 fusion proteins; foot-and-mouth disease virus; OmpA; cell surface exposure; major antigenic domain; immune responses; Performance evaluation; Immunoprotection; Antigen presentation; Immunization; Heterologous system; Antigenic determinant; Picornaviridae; Escherichia coli; Rabbit; Shigella dysenteriae; Lagomorpha; External membrane; Cell surface; Virus; Aphthovirus; Vertebrata; Mammalia; Bacteria; Enterobacteriaceae
• ISSN: 0264-410X; 1873-2518
• DOI: 10.1016/0264-410X(94)90305-0

Exposure at the bacterial outer surface of the major antigenic epitope of the foot-and-mouth disease (FMDV) viral protein VP1 was studied using protein fusion with outer membrane protein A (OmpA) of Shigella dysenteriae for production and transport of the foreign polypeptide to the outer membrane of Escherichia coli. Fusion constructs with VP1 peptide insertions of up to 56 amino acids in the third outer domain of OmpA could be demonstrated on the bacterial surface by indirect immunofluorescence and immunogold labelling. OmpA fusion proteins with large insertions from sequences of the FMDV protein VP1 were shown to elicit virus-specific immune responses in rabbits.