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• W2010014786 abstract "Eight surface-radioiodinated merozoite proteins from a cloned, pathogenic isolate of Babesia bovis can be immunoprecipitated by antibody from cattle that are completely protected against clinical babesiosis. Among these eight surface proteins, the 55- and 42-kDa molecules are biosynthetically labeled with [3H]glucosamine. The 42-kDa glycoprotein can also be labeled with [3H]myristic acid and partitions exclusively into the detergent phase in Triton X-114 extracts, indicating that it is an integral membrane protein and suggesting that it is anchored by a glycosylphosphatidylinositol moiety. Antibody-mediated protection against B. bovis merozoites most probably requires a high level of circulating antibody to ensure antibody-merozoite binding during the parasite's brief extraerythrocytic phase. Antibodies in diluted sera selectively recognize the 120-, 85-, 55- and 42-kDa surface proteins. Only the 42-kDa integral membrane protein is reactive with serum antibodies diluted ⩾ 1:16 000. Thus, we hypothesize that these immunodominant proteins, especially the transmembrane 42-kDa glycoprotein, are important to the induction of the protective immune response and are candidates for an improved vaccine against babesiosis." @default.
• W2010014786 created "2016-06-24" @default.
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• W2010014786 date "1989-11-01" @default.
• W2010014786 modified "2023-10-16" @default.
• W2010014786 title "Molecular characterization of Babesia bovis merozoite surface proteins bearing epitopes immunodominant in protected cattle" @default.
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• W2010014786 doi "https://doi.org/10.1016/0166-6851(89)90096-0" @default.
• W2010014786 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/2482443" @default.
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