Characterisation of a family of multi-copy genes encoding rhoptry protein homologues in Babesia bovis, Babesia ovis and Babesia canis

Dalrymple, Brian P.; Casu, Rosanne E.; Peters, Jennifer M.; Dimmock, Christine M.; Gale, K. R.; Boese, Reinhard; Wright, I.G.

doi:10.1016/0166-6851(93)90194-3

Cited by 66 publications

(40 citation statements)

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“…For the purification of B. bovis merozoites, infected Bo-RBC were treated with 0.83% NH 4 Cl solution for 10 min at 37°C and then washed three times with cold PBS (13). Similarly, Sf9 insect cells were seeded on an 80-cm 2 of pepstatin A and leupeptin per ml), incubated on ice for 20 min, and then centrifuged at 18,000 ϫ g for 30 min at 4°C.…”

Section: Methodsmentioning

confidence: 99%

“…The rhoptry-associated protein 1 (RAP-1) of B. bovis merozoites bears substantial sequence homology to the RAP-1 of other Babesia parasites (3,4) and contains immunogenic B-cell epitopes (20), and the purified recombinant RAP-1 has proven effective in inducing protective immunity in the vaccinated cattle (22). All of these earlier findings point to the biological and immunological characteristics of RAP-1 that would justify its inclusion in a recombinant vaccine to prevent B. bovis infection.…”

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confidence: 99%

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Cellular Localization of Babesia bovis Merozoite Rhoptry-Associated Protein 1 and Its Erythrocyte-Binding Activity

et al. 2002

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The cellular localization of Babesia bovis rhoptry-associated protein 1 (RAP-1) and its erythrocyte-binding affinity were examined with anti-RAP-1 antibodies. In an indirect immunofluorescent antibody test, RAP-1 was detectable in all developmental stages of merozoites and in extracellular merozoites. In the early stage of merozoite development, RAP-1 appears as a dense accumulation, which later thins out and blankets the host cell cytoplasm, but retains a denser mass around newly formed parasite nuclei. The preferential accumulations of RAP-1 on the inner surface of a host cell membrane and bordering the parasite's outer surface were demonstrable by immunoelectron microscopy. An erythrocyte-binding assay with the lysate of merozoites demonstrated RAP-1 binding to both bovine and equine erythrocytes. Anti-RAP-1 monoclonal antibody 1C1 prevented the interaction of RAP-1 with bovine erythrocytes and significantly inhibited parasite proliferation in vitro. With the recombinant RAP-1, the addition of increasing concentrations of Ca 2؉ accentuated its binding affinity with bovine erythrocytes. The present findings lend support to an earlier proposition of an erythrocytic binding role for RAP-1 expressed in B. bovis merozoites and, possibly, its involvement in the escape of newly formed merozoites from host cells.Babesia bovis is a hemoprotozoan parasite that causes great economic losses to the cattle industry worldwide. It is transmitted by tick vectors and has an asexual intraerythrocytic cycle in the infected cattle (5, 9). Understanding the basic molecular mechanism(s) of the asexual intraerythrocytic cycle, particularly the process of merozoite invasion into and escape from infected erythrocytes (RBC), may accelerate the development of an effective vaccine. Extracellular merozoites are directly exposed to the host humoral immune components. Consequently, efforts to identify potential components for the development of a vaccine are primarily directed at the merozoite stage.Apicomplexans utilize several rhoptry proteins in their invasion into and development within the host cell (16, 18). Extracellular merozoites attach to the host RBC and reorient to bring the apical organelles close to the attachment interface, and through the interaction of protozoan ligands with several surface receptors, the rhoptry products are released at the point of membrane invagination. Although the morphological events during host cell recognition and penetration appear to be similar among the apicomplexans, some molecular events mediated by each secretory component of the rhoptry vary and are unique (16,18).The rhoptry-associated protein 1 (RAP-1) of B. bovis merozoites bears substantial sequence homology to the RAP-1 of other Babesia parasites (3, 4) and contains immunogenic B-cell epitopes (20), and the purified recombinant RAP-1 has proven effective in inducing protective immunity in the vaccinated cattle (22). All of these earlier findings point to the biological and immunological characteristics of RAP-1 that would justify its inc...

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confidence: 99%

Cellular Localization of Babesia bovis Merozoite Rhoptry-Associated Protein 1 and Its Erythrocyte-Binding Activity

et al. 2002

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“…B. bovis RAP-1 is the product of a member of a multigene family encoding 58-to 60-kDa proteins identified in Babesia bigemina, Babesia canis, Babesia divergens, Babesia ovis, and Babesia caballi parasites (13,14,22,23,33,34,37). RAP-1 is highly conserved among otherwise antigenically variant strains of B. bovis.…”

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confidence: 99%

“…The NT region contains four cysteine residues and additional amino acid motifs that are highly conserved among RAP-1 orthologs from the different species of Babesia (12,13,33,38). The presence of such conserved amino acid motifs in the NT region of RAP-1 indicates that the region is functionally important and may therefore be useful as a target of immune intervention (38).…”

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confidence: 99%

Stimulation of T-Helper Cell Gamma Interferon and Immunoglobulin G Responses Specific forBabesia bovisRhoptry-Associated Protein 1 (RAP-1) or a RAP-1 Protein Lacking the Carboxy-Terminal Repeat Region Is Insufficient To Provide Protective Immunity against VirulentB. bovisChallenge

Norimine¹,

Mosqueda²,

Suárez

et al. 2003

Infect Immun

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“…bovis RAP-1 is a member of a family of 58-to 60-kDa proteins of multiple genes that have also been identified in Babesia bigemina, Babesia caballi, Babesia canis, Babesia divergens, and Babesia ovis parasites (17,18,27,33,37,40). In B. bovis, RAP-1 is encoded by two nearly identical genes and consists of a unique N-terminal (NT) region (amino acids [aa] 1 to 316) and a C-terminal (CT) region (aa 317 to 565) that contains seven tandem repeats of a degenerate 23-aa sequence ( Fig.…”

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Immunodominant Epitopes inBabesia bovisRhoptry-Associated Protein 1 That Elicit Memory CD4⁺-T-Lymphocyte Responses inB. bovis-Immune Individuals Are Located in the Amino-Terminal Domain

et al. 2002

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Babesia bovis rhoptry-associated protein 1 (RAP-1), which confers partial protection against B. bovis challenge, is recognized by antibodies and T lymphocytes from cattle that have recovered from infection and are immune to subsequent challenge. RAP-1 is a 60-kDa protein with an N-terminal (NT) region that contains four cysteine residues conserved among all Babesia RAP-1 family members and a C-terminal (CT) region that contains multiple, degenerate, tandem 23-amino-acid (aa) repeats. To define the location of CD4؉ -T-cell epitopes for vaccine development using a recombinant protein or minigene construct, a series of truncated recombinant RAP-1 proteins and peptides were tested for stimulation of T-cell lines derived from B. bovisimmune cattle.

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Characterisation of a family of multi-copy genes encoding rhoptry protein homologues in Babesia bovis, Babesia ovis and Babesia canis

Cited by 66 publications

References 31 publications

Cellular Localization of Babesia bovis Merozoite Rhoptry-Associated Protein 1 and Its Erythrocyte-Binding Activity

Cellular Localization of Babesia bovis Merozoite Rhoptry-Associated Protein 1 and Its Erythrocyte-Binding Activity

Stimulation of T-Helper Cell Gamma Interferon and Immunoglobulin G Responses Specific forBabesia bovisRhoptry-Associated Protein 1 (RAP-1) or a RAP-1 Protein Lacking the Carboxy-Terminal Repeat Region Is Insufficient To Provide Protective Immunity against VirulentB. bovisChallenge

Immunodominant Epitopes inBabesia bovisRhoptry-Associated Protein 1 That Elicit Memory CD4⁺-T-Lymphocyte Responses inB. bovis-Immune Individuals Are Located in the Amino-Terminal Domain

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Characterisation of a family of multi-copy genes encoding rhoptry protein homologues in Babesia bovis, Babesia ovis and Babesia canis

Cited by 66 publications

References 31 publications

Cellular Localization of Babesia bovis Merozoite Rhoptry-Associated Protein 1 and Its Erythrocyte-Binding Activity

Cellular Localization of Babesia bovis Merozoite Rhoptry-Associated Protein 1 and Its Erythrocyte-Binding Activity

Stimulation of T-Helper Cell Gamma Interferon and Immunoglobulin G Responses Specific forBabesia bovisRhoptry-Associated Protein 1 (RAP-1) or a RAP-1 Protein Lacking the Carboxy-Terminal Repeat Region Is Insufficient To Provide Protective Immunity against VirulentB. bovisChallenge

Immunodominant Epitopes inBabesia bovisRhoptry-Associated Protein 1 That Elicit Memory CD4+-T-Lymphocyte Responses inB. bovis-Immune Individuals Are Located in the Amino-Terminal Domain

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Immunodominant Epitopes inBabesia bovisRhoptry-Associated Protein 1 That Elicit Memory CD4⁺-T-Lymphocyte Responses inB. bovis-Immune Individuals Are Located in the Amino-Terminal Domain