Immunogenicity of a foreign peptide expressed within a capsid protein of an attenuated coxsackievirus
Autor: | Arlene I. Ramsingh, Stephanie E. Ostrowski, Sadia S. Halim, William T. Lee |
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Rok vydání: | 2000 |
Předmět: |
Ovalbumin
viruses T-Lymphocytes Genetic Vectors Molecular Sequence Data DNA Recombinant Coxsackievirus In Vitro Techniques Recombinant virus Lymphocyte Activation Transfection Virus Replication Epitope Cell Line Mice Capsid medicine Animals Amino Acid Sequence Peptide sequence Mice Inbred BALB C General Veterinary General Immunology and Microbiology biology Base Sequence Chimera Immunogenicity Public Health Environmental and Occupational Health T helper cell biology.organism_classification Virology Molecular biology Recombinant Proteins Enterovirus B Human Infectious Diseases medicine.anatomical_structure Helper virus Molecular Medicine |
Zdroj: | Vaccine. 19(7-8) |
ISSN: | 0264-410X |
Popis: | The immunogenicity of soluble peptides can be improved by expression within recombinant microorganisms. The immunogenicity of a peptide expressed within a capsid protein of an attenuated coxsackievirus B4 was evaluated. The insertion site was chosen based on its antigenic structure. A foreign peptide was inserted into a region of the VP1 capsid protein that was identified as a T helper cell epitope. A recombinant virus containing ten amino acids of ovalbumin sequence was genetically stable and retained the biological and physical characteristics of the parental virus. The recombinant was able to elicit a T helper cell response against ovalbumin sequences. This study shows, for the first time, that coxsackievirus can be used as an expression vector and that insertion of heterologous peptides into an immunogenic region is a viable strategy for inducing T helper cell responses against foreign sequences. The implications of this work are that the attenuated coxsackievirus variant may be useful as a vaccine vector for expressing T helper cell epitopes that are important in inducing protective immunity. |
Databáze: | OpenAIRE |
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