The gene defective in X-linked lymphoproliferative disease controls T cell dependent immune surveillance against Epstein–Barr virus

• Published in: Current Opinion in Immunology Vol. 12; no. 4; pp. 474 - 478
• Main Authors: Howie, Duncan, Sayos, Juan, Terhorst, Cox, Morra, Massimo
• Format: Book Review Journal Article
• Language: English
• Published: England Elsevier Ltd 01-08-2000
• Subjects: Antigens, CD; Binding motif; Carrier Proteins - genetics; Carrier Proteins - immunology; Cloning, Molecular; Crystal structure; Epstein-Barr virus; Gene Deletion; Glycoproteins - immunology; Herpesvirus 4, Human - immunology; Human; Humans; Immunoglobulins - immunology; Intracellular Signaling Peptides and Proteins; Lymphoproliferative; Lymphoproliferative Disorders - genetics; Lymphoproliferative Disorders - immunology; Lymphoproliferative Disorders - virology; Receptors, Antigen, T-Cell - immunology; Receptors, Cell Surface; SAP; SAP gene; SH2; SH21A/SAP gene; SHD1A; Signaling Lymphocytic Activation Molecule Associated Protein; Signaling Lymphocytic Activation Molecule Family Member 1; SLAM; T-Lymphocytes - immunology; X-linked lymphoproliferative disease; X-linked lymphoproliferative syndrome; XLP; Human; Immunology; SAP; SLAM; Lymphoproliferative; Genetics; Binding motif; SHD1A; SH2; XLP; Crystal structure
• ISSN: 0952-7915; 1879-0372
• DOI: 10.1016/S0952-7915(00)00123-0

Our understanding of the X-linked lymphoproliferative syndrome (XLP) has advanced significantly in the past two years. The gene that is aberrant in the condition –
SH2D1A/
SAP, which encodes SAP (signaling lymphocytic activation molecule [SLAM]-associated protein) – was cloned, the crystal structure of its product was solved and insights into the signaling mechanisms of this small SH2-domain-containing protein via the cell surface receptors SLAM and 2B4 have been provided.
SAP mutation, and not Epstein–Barr virus infection per se, may be critical for XLP.