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Expression and characterization of loop‐ and helix‐forming epitopes of measles virus hemagglutinin in plants
Author(s) -
Sulima Sergey,
Musiychuk Konstantin,
Bouche Fabienne B.,
Muller Claude P.,
Yusibov Vidadi,
Mett Vadim
Publication year - 2008
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.22.1_supplement.1068.5
Subject(s) - epitope , measles virus , virology , nicotiana benthamiana , hemagglutinin (influenza) , antigen , biology , antibody , virus , measles , vaccination , immunization , antigenicity , microbiology and biotechnology , immunology
The number of cases of acute Measles Virus (MV) in the United States plummeted 98% since 1963, when a live attenuated vaccine has been introduced. However, such a vaccine requires constant refrigeration to preserve potency. More importantly, the presence of maternal antibodies interferes with effectiveness of the vaccine before ~9 months of age. These reasons present a major impediment for the vaccination of young children, especially in developing countries. Here, we report the transient expression of two MV hemagglutinin epitopes in Nicotiana benthamiana . These loop‐ (L) and helix‐ (H) forming epitopes are not recognized by maternal antibodies, have been shown to generate a protective immune response in mice, and could be used to develop a vaccine for infants before the age of 9 months. The epitopes were fused to the surface loop of the thermostable enzyme of Clostridium thermocellum , and produced in plants through a combination of viral and bacterial vectors. Purified antigens were characterized by SDS‐PAGE followed by immunoblotting. Immunological testing showed that the L‐ and H‐epitopes are recognized by L‐ and H‐specific antibodies, respectively, thus successfully mimicking natural antigenic properties.