Strain variation of Babesia bovis merozoite surface-exposed epitopes.
نویسندگان
چکیده
Babesia bovis merozoites are exposed to antibodies during the extraerythrocytic phase, and surface polypeptides bearing exposed epitopes are possible immunogens. Monoclonal antibodies reactive with the merozoite surface bind either immunodominant epitopes expressed diffusely on the merozoite surface or, alternatively, epitopes expressed in a polar pattern. Epitopes expressed diffusely on the immunodominant 42- and 44-kDa merozoite polypeptides were not conserved among strains from geographically diverse regions. In contrast, epitopes expressed in a polar pattern on the merozoite surface were conserved among nine strains and clones. Identification of variables and conserved epitopes provides a basis for defining antigenic variation and cross-protective immunity.
منابع مشابه
In silico predicted conserved B-cell epitopes in the merozoite surface antigen-2 family of B. bovis are neutralization sensitive.
The merozoite surface antigens MSA-2 of Babesia bovis constitute a family of polymorphic GPI-anchored glycoproteins located at the parasite cell surface, that contain neutralization-sensitive B-cell epitopes. These are therefore putative vaccine candidates for bovine babesiosis. It was previously shown that (i) the MSA-2 antigens of the biologically cloned Mo7 strain are encoded by four tandeml...
متن کاملSequence variation and immunologic cross-reactivity among Babesia bovis merozoite surface antigen 1 proteins from vaccine strains and vaccine breakthrough isolates.
The Babesia bovis merozoite surface antigen 1 (MSA-1) is an immunodominant membrane glycoprotein that is the target of invasion-blocking antibodies. While antigenic variation has been demonstrated in MSA-1 among strains from distinct geographical areas, the extent of sequence variation within a region where it is endemic and the effect of variation on immunologic cross-reactivity have not been ...
متن کاملBabesia bovis rhoptry-associated protein 1 is immunodominant for T helper cells of immune cattle and contains T-cell epitopes conserved among geographically distant B. bovis strains.
The ability of rhoptry-associated protein 1 (RAP-1) of Babesia bovis and Babesia bigemina to confer partial protective immunity in cattle has stimulated interest in characterizing both B-cell and T-cell epitopes of these proteins. It was previously shown that B. bovis RAP-1 associates with the merozoite surface as well as rhoptries and expresses B-cell epitopes conserved among otherwise antigen...
متن کاملImmunogenic B-cell epitopes of Babesia bovis rhoptry-associated protein 1 are distinct from sequences conserved between species.
Babesia bovis merozoite apical membrane polypeptide Bv60 was found to be rhoptry associated by immuno-electron microscopy and was redesignated rhoptry-associated protein 1 (RAP-1). The N-terminal 300 amino acids of RAP-1 have a high level of sequence similarity to the same N-terminal region of p58, its homolog from Babesia bigemina. However, the interspecies conserved sequences did not include ...
متن کاملThe Babesia bovis merozoite surface antigen 1 hypervariable region induces surface-reactive antibodies that block merozoite invasion.
A hypervariable region (HVR) previously identified in the carboxy-terminal one-third of the Babesia bovis variable merozoite surface antigen family was more extensively analyzed in merozoite surface antigen 1 (MSA-1) from 16 strains and isolates. The MSA-1 HVR is proline rich and contains three semiconserved motifs nearly identical to those described for the related family member MSA-2. Two MSA...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید
ثبت ناماگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید
ورودعنوان ژورنال:
- Infection and immunity
دوره 59 9 شماره
صفحات -
تاریخ انتشار 1991