The study shows that a protein from cholera (CT‑B) sticks tightly to immune cells, and that the immune‑boosting peptide thymosin‑alpha‑1 (and a short mimic peptide) can block this binding. Both the cholera protein and the short peptide also raise an enzyme activity (soluble guanylate cyclase) inside the cells, which could affect cell signaling.

We have prepared ¹²⁵I-labeled cholera toxin B subunit (¹²⁵I-labeled CT-B, a specific activity of 98Ci/mmol) and found that its binding to T and B lymphocytes from the blood of healthy donors was high-affinity (K_d 2.8 and 3.0nM, 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 (K_i>10μM). 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 10-1000nM increased in a dose-dependent manner the soluble guanylate cyclase activity in T and B lymphocytes.