The immunosuppressant cyclosporin A (CsA) forms a trimolecular complex with cyclophilin and calcineurins to inhibit calcineurin phosphatase activity (1). Cyclophilins are conserved, ubiquitous and abundant cytosolic peptidyl-prolyl cis-trans isomerases that accelerate the isomerization of XaaPro peptide bonds and the refolding of proteins (2,3). Human cyclophilin A (CyPA), an intracellular protein of 165 amino acids, is the target of the CsA and is encoded by a single unique gene conserved from yeast to humans (4,5). CyPA is known for its involvement in T cell differentiation and proliferation and is highly expressed in brain (6). CyPA is incorporated into the virion of the type 1 human immunodeficiency virus (HIV-1) via a direct interaction with the capsid domain of the viral Gag polyprotein and is crucial for efficient viral replication (7,8). Cyclophilin B (CyPB) is a member of the cyclophilin family with specific N- and C-terminal extensions. Unlike CyPA, CyPB has a signal sequence leading to its translocation in the endoplasmic reticulum. CyPB is secreted in biological fluids such as blood or milk and binds to a specific receptor present on the human lymphoblastic cell line Jurkat and on human peripheral blood lymphocytes (9,10).