Genetic and antigenic characterization of Babesia bovis merozoite spherical body protein Bb-1.

Abstract:

:A Babesia bovis merozoite protein, Bb-1, was localized by immunoelectron microscopy to an apical organelle known as the spherical body. This unique structure appears to be analogous to dense granules of other apicomplexan protozoa. Similar to previously described dense granule proteins of Plasmodium spp., Bb-1 is secreted during or just after invasion of host erythrocytes and becomes associated with the cytoplasmic face of the infected cell. The amino terminal sequence of Bb-1 contains a predicted signal peptide and is similar to the amino terminus of another spherical body protein (BvVA1/225) which is also translocated to the erythrocyte membrane. Importantly, these two spherical body proteins are the major components of a protective fraction of B. bovis antigen. There is marked conservation of Bb-1 amino acid sequences and B-lymphocyte epitopes among geographic strains. However, a divergent Bb-1 allele (Bv80) in Australia strains encodes six regions of amino acid polymorphism, including a region of tetrapeptide repeats in the C-terminal half of the polypeptide. Two of the polymorphic regions map to previously defined Th1 epitopes on Bb-1.

journal_name

Mol Biochem Parasitol

authors

Hines SA,Palmer GH,Brown WC,McElwain TF,Suarez CE,Vidotto O,Rice-Ficht AC

doi

10.1016/0166-6851(94)00200-7

subject

Has Abstract

pub_date

1995-02-01 00:00:00

pages

149-59

issue

2

eissn

0166-6851

issn

1872-9428

pii

0166685194002007

journal_volume

69

pub_type

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