The effect of immune serum and complement on the in vitro phagocytosis of Babesia rodhaini

Parrodi, F.; Jacobson, Richard H.; Wright, I.G.; Fitzgerald, C. J.; Dobson, Colin

doi:10.1111/j.1365-3024.1991.tb00544.x

Cited by 13 publications

(5 citation statements)

References 31 publications

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“…These antibodies also caused phagocytosis of infected erythrocytes by cultured bovine monocytes. A positive correlation between the opsonin titer and protective activity against Babesia rodhaini in rats occurs (23). Studies of B. bovis (9,10,15), Babesia equi (13), and Babesia canis (28) infections indicate that phagocytosis of infected erythrocytes by peripheral blood leukocytes is involved in the resolution of infections.…”

Section: Discussionmentioning

confidence: 99%

Monoclonal antibody to a conserved epitope on proteins encoded by Babesia bigemina and present on the surface of intact infected erythrocytes

et al. 1995

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To define Babesia bigemina-specific antigens on the surface of infected erythrocytes, monoclonal antibodies (MAbs) were identified by live-cell immunofluorescence. As determined by live-cell immunofluorescence, two MAbs made to the Mexico strain reacted with the Mexico strain and three Kenya strains, while three MAbs made to the Kenya-Ngong strain reacted with the Kenya strains but not the Mexico strain. Binding of MAb 44.18 (made to the Mexico strain) to a strain-common epitope was confirmed by immunoelectron microscopy and by surface-specific immunoprecipitation of [ 35 S]methionine-labeled proteins (200, 28, and 16 kDa in size), which also demonstrated that the MAb recognized an epitope on proteins encoded by B. bigemina. In immunoblots, the MAb bound to predominant antigens with sizes of 200 and 220 kDa in erythrocyte lysates infected with strains from Puerto Rico, St. Croix, Texcoco (Mexico), Kenya, and Mexico. Major antigens with sizes of 200 and 220 kDa were isolated from a MAb 44.18 affinity matrix. Calf serum antibodies to these isolated antigens bound to erythrocytes infected with either the Mexico or Kenya strains as determined by live-cell immunofluorescence, allowing the conclusion that at least one conserved surface epitope was recognized. Calf serum antibodies identified major labeled proteins with sizes of 200 and 72 kDa by surface-specific immunoprecipitation, and infected erythrocytes sensitized with these antibodies were phagocytized by cultured bovine peripheral blood monocytes. These results provide a rationale for evaluating antigens identified by MAb 44.18 individually and as components of subunit vaccines.

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Section: Discussionmentioning

confidence: 99%

Monoclonal antibody to a conserved epitope on proteins encoded by Babesia bigemina and present on the surface of intact infected erythrocytes

et al. 1995

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“…On the contrary, it has been observed that several components of the complement pathway are essential in the invasion of erythrocytes by B. rodhaini (31). Also, in a study in which complement was used to promote macrophage phagocytosis of B. rodhaini merozoites, the unexpected finding was that the presence of complement inhibited phagocytosis of the pathogen (157).…”

Section: Host Immune Responsementioning

confidence: 96%

Babesiosis

Homer¹,

Aguilar-Delfín²,

Telford³

et al. 2000

Clinical Microbiology Reviews

522

402

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“…(37) showed that the complement, in the presence of an immune serum, does not reproducibly enhance the phagocytosis of infected erythrocytes with B. rodhaini or parasites alone in vitro . The depletion of serum C3 does not affect the course of B. rodhaini in BALB/C mice (37). Likewise, the complement does not have a role in the entry of B. bovis into the RBC in vitro (39).…”

Section: Research Notementioning

confidence: 99%

C3 contributes to the cross‐protective immunity induced by Babesia gibsoni phosphoriboprotein P0 against a lethal B. rodhaini infection

Terkawi

Zhang

Jia

et al. 2008

Parasite Immunology

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We have studied the impact of complement component 3 (C3) deficiency on the progression of lethal Babesia rodhaini infection in immune mice. A B. gibsoni ribosomal phosphoprotein P0 (BgP0) previously reported to be a cross-protective antigen against Babesia infection was used to immunize C57BL/6 wild-type (WT) and C3-deficient (C3-/-) mice. Test mice were immunized intraperitoneally (i.p.) with recombinant BgP0 (rBgP0), while controls either were immunized with PBS or did not receive any immunization. Following the immunization regime, test WT mice induced a specifically strong humoral response consisting of mixed immunoglobulins IgG1 and IgG2 associated with high production of IFN-gamma in the supernatant of splenocytes. While test C3-/- mice had significantly decreased total IgG, IgG1 and IgG2b responses, the secretions of IL-12 and IFN-gamma tended to be lower than those in WT mice. Furthermore, partial protection was only observed in rBgP0-immunized WT mice but not in C3-/- mice or controls. Indeed, rBgP0-immunized WT mice showed significant reductions in the initiation of parasitaemia correlated with delayed mortalities and considerable survival rates. Taken together, our results indicate that cross-protection was impaired in C3-/- mice in view of the decrease in the antibody responses and cytokine production and the high susceptibility to infection.

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The effect of immune serum and complement on the in vitro phagocytosis of Babesia rodhaini

Cited by 13 publications

References 31 publications

Monoclonal antibody to a conserved epitope on proteins encoded by Babesia bigemina and present on the surface of intact infected erythrocytes

Monoclonal antibody to a conserved epitope on proteins encoded by Babesia bigemina and present on the surface of intact infected erythrocytes

Babesiosis

C3 contributes to the cross‐protective immunity induced by Babesia gibsoni phosphoriboprotein P0 against a lethal B. rodhaini infection

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