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Individual antigens of cattle. Bovine CD2 (BoCD2)
1Department of Veterinary Microbiology/Pathology, Washington State University, Pullman 99164-7040.
Insights
New monoclonal antibodies (mAbs) recognize the bovine CD2 molecule, inhibiting rosetting and identifying its presence on T-cells. Further research is needed to fully characterize these CD2 epitopes and activation pathways.
Area of Science:
- Immunology
- Veterinary Immunology
- Cell Biology
Background:
- CD2 is a crucial cell surface glycoprotein involved in lymphocyte activation.
- Understanding bovine CD2 (BoCD2) is essential for comparative immunology and veterinary applications.
- Previous studies have identified some aspects of BoCD2 but a comprehensive characterization is lacking.
Purpose of the Study:
- To characterize new monoclonal antibodies (mAbs) targeting the bovine CD2 molecule.
- To investigate the cellular expression and functional properties of BoCD2.
- To compare BoCD2 epitopes and activation mechanisms with human CD2.
Main Methods:
- Workshop-based analysis of 14 new mAbs (CH128A, IL-A26, and 12 others) against bovine cells.
- Assays included rosetting inhibition with sheep red blood cells (SRBC).
- Immunoprecipitation of cell surface proteins and flow cytometry for cell staining.
Main Results:
- The mAbs recognize the bovine orthologue of CD2 (BoCD2).
- BoCD2 is expressed on the majority of CD4+ and CD8+ T-cells and a small population of CD4-/CD8- cells in cattle.
- The mAbs immunoprecipitate a peptide of 58-62 kDa, consistent with CD2.
Conclusions:
- The new mAbs provide valuable tools for studying BoCD2.
- BoCD2 expression patterns in cattle are largely consistent with human CD2.
- Further studies are required to define epitope mapping and functional activation differences compared to human CD2.
Abstract:
The data obtained in the workshop provide further evidence that CH128A and IL-A26 and the 12 new mAbs that form a cluster recognise the bovine orthologue of CD2. The mAbs inhibit rosetting with SRBC, stain cells in primary and secondary lymphoid organs in patterns consistent with those obtained in humans with anti-CD2 mAbs, and the 11 IgG mAbs all immunoprecipitate a peptide with a Mr of 58-62 kDa. It is not clear from the studies whether the epitopes defined by the mAbs correspond with the region I and II epitopes present on CD2. None of the data suggest that any of the mAbs recognise the region III (CDD2R) epitope (Peterson and Seed, 1987; Knapp et al., 1989). Further studies are now needed to define the physical and functional relation of the epitopes and establish whether antibody-mediated activation corresponds with that noted in humans. Data reported in one study (Baldwin et al., 1988) with IL-A26 suggest possible differences in the requirements for activation. In addition, further studies are needed to demonstrate how many cell types express BoCD2. In mice, evidence has been presented which shows the mouse orthologue is expressed on some B cells (Yagitta et al., 1989). Studies in cattle have clearly shown CD2 is present on the majority of CD4+ and CD8+ T-cells and a small population of CD4-/CD8- cells (Baldwin et al., 1988; Davis, unpublished observations). Evidence presented in this workshop has shown that some CD2+ cells express a WC2 molecule (Sopp et al., 1991).(ABSTRACT TRUNCATED AT 250 WORDS)