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Related Experiment Videos

Conformational changes in CD45 upon monoclonal antibody crosslinking

D Hamann1, W Eichler, H Fiebig

  • 1Central Laboratory of the Netherlands, Red Cross Blood Transfusion Service, University of Amsterdam.

Hybridoma
|February 1, 1996
PubMed
Summary

Researchers identified a new CD45 epitope recognized by MAb BL-TSub/2. This epitope

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Area of Science:

  • Immunology
  • Molecular Biology
  • Cell Biology

Background:

  • CD45 protein tyrosine phosphatase exists in various isoforms due to alternative splicing of exons A, B, and C.
  • These isoforms affect the N-terminus of the extracellular domain of CD45.
  • Understanding CD45 isoforms is crucial for immune cell function and signaling.

Purpose of the Study:

  • To characterize a novel epitope on the N-terminal end of CD45.
  • To investigate the binding properties of the monoclonal antibody (MAb) BL-TSub/2.
  • To explore the relationship between the BL-TSub/2 epitope and other known CD45 epitopes.

Main Methods:

  • Utilized monoclonal antibody (MAb) BL-TSub/2 for epitope mapping.
  • Performed crossblocking studies with UCHL1 (CD45RO) antibody.
  • Assessed epitope sensitivity to protease and neuraminidase treatments.
  • Investigated the effect of CD45 common and CD45RA MAb preincubation on BL-TSub/2 binding.

Main Results:

  • A novel CD45 epitope recognized by MAb BL-TSub/2 was identified.
  • The BL-TSub/2 and CD45RO epitopes showed partial overlap.
  • BL-TSub/2 binding was sensitive to protease treatment but involved carbohydrate moieties, similar to CD45RO.
  • Crosslinking CD45 molecules (via CD45 common and CD45RA MAb) enhanced BL-TSub/2 binding, suggesting conformational changes.

Conclusions:

  • The novel BL-TSub/2 epitope is distinct from the CD45RO epitope, particularly in its sensitivity to proteases.
  • The epitope's dependence on carbohydrate moieties and its modulation by CD45 crosslinking provide insights into CD45 structure and function.
  • These findings suggest that CD45 crosslinking may induce conformational changes affecting ligand interactions.

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