Interaction of cholera toxin B subunit with T and B lymphocytes

- Cholera toxin B subunit binds with high affinity to human T and B lymphocytes.
- TM-α1, INF-α2, peptide LKEKK completely inhibit the cholera toxin B subunit binding.
- Residues 16-20 in TM-α1 and 131-135 in IFN-α2 are involved in binding to the receptor.
- Binding to the receptor leads to an increase in activity of soluble guanylate cyclase.

We have prepared 125I-labeled cholera toxin B subunit (125I-labeled CT-B, a specific activity of 98 Ci/mmol) and found that its binding to T and B lymphocytes from the blood of healthy donors was high-affinity (Kd 2.8 and 3.0 nM, respectively). The binding of labeled protein was completely inhibited by unlabeled thymosin-α1 (TM-α1), interferon-α2 (IFN-α2), and the synthetic peptide LKEKK that corresponds to residues 16-20 in TM-α1 and 131-135 in IFN-α2, but was not inhibited by the synthetic peptide KKEKL with inverted amino acid sequence (Ki > 10 μM). Thus, TM-α1, IFN-α2, and the peptide: LKEKK bind with high affinity and specificity to CT-B receptor on donor blood T and B lymphocytes. It was found that CT-B and the peptide: LKEKK at concentrations of 10-1000 nM increased in a dose-dependent manner the soluble guanylate cyclase activity in T and B lymphocytes.

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