A Schistosoma mansoni Fatty Acid-Binding Protein, Sm14, is the Potential Basis of a Dual-Purpose Anti-Helminth Vaccine

Molecular cloning of components of protective antigenic preparations has suggested that related parasite fatty acid-binding proteins could form the basis of the protective immune crossreactivity between the parasitic trematode worms Fasciola hepatica and Schistosoma mansoni. Molecular models of the...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 1996-01, Vol.93 (1), p.269-273
Main Authors: Tendler, Miriam, Brito, Cristiana A., Vilar, Monica Magno, Serra-Freire, Nicolau, Diogo, Catia M., Almeida, Marilia S., Alexandre C. B. Delbem, Da Silva, José Figueiredo, Savino, Wilson, Garratt, Richard C., Katz, Naftale, Andrew J. G. Simpson
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Amino acids
Animals
Antigens, Helminth - immunology
Carrier Proteins
Cercariae
Cross Reactions
Epitope Mapping
Epitopes
Fasciola hepatica
Fasciola hepatica - immunology
Fatty acid binding proteins
Fatty Acid Transport Proteins
Helminth Proteins - immunology
Humans
Immunity (Disease)
Infections
Liver
Medical research
Membrane Transport Proteins
Mice
Models, Molecular
Molecular Sequence Data
Molecules
Parasites
Proteins
Rabbits
Schistosoma mansoni
Schistosoma mansoni - chemistry
Schistosoma mansoni - immunology
Schistosomiasis mansoni - prevention & control
Sequence Alignment
Sequence Homology, Amino Acid
Vaccination
Vaccines
Vaccines, Synthetic
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Summary:Molecular cloning of components of protective antigenic preparations has suggested that related parasite fatty acid-binding proteins could form the basis of the protective immune crossreactivity between the parasitic trematode worms Fasciola hepatica and Schistosoma mansoni. Molecular models of the two parasite proteins showed that both molecules adopt the same basic three-dimensional structure, consisting of a barrel-shaped molecule formed by 10 antiparallel β -pleated strands joined by short loops, and revealed the likely presence of crossreactive, discontinuous epitopes principally derived from amino acids in the C-terminal portions of the molecules. A recombinant form of the S. mansoni antigen, rSm14, protected outbred Swiss mice by up to 67% against challenge with S. mansoni cercariae in the absence of adjuvant and without provoking any observable autoimmune response. The same antigen also provided complete protection against challenge with F. hepatica metacercariae in the same animal model. The results suggest that it may be possible to produce a single vaccine that would be effective against at least two parasites, F. hepatica and S. mansoni, of veterinary and human importance, respectively.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.93.1.269