Proline-serine-threonine phosphatase interacting protein 1 (PSTPIP1) controls immune synapse stability in human T cells.

Background: Proline-serine-threonine phosphatase interacting protein 1 (PSTPIP1) is a cytosolic adaptor protein involved with T-cell activation, differentiation, and migration. On cognate T-cell contact, PSTPIP1 is recruited to surface-expressed CD2, where it regulates F-actin remodeling. An immune synapse (IS) is thereby rapidly formed, consisting of T-cell receptor clusters surrounded by a ring of adhesion molecules, including CD2.

Neonatal thymectomy reveals differentiation and plasticity within human naive T cells.

The generation of naive T cells is dependent on thymic output, but in adults, the naive T cell pool is primarily maintained by peripheral proliferation. Naive T cells have long been regarded as relatively quiescent cells; however, it was recently shown that IL-8 production is a signatory effector function of naive T cells, at least in newborns. How this functional signature relates to naive T cell dynamics and aging is unknown.

Antigen-specific IgA titres after 23-valent pneumococcal vaccine indicate transient antibody deficiency disease in children.

Paediatric patients with antibody deficiency may either be delayed in development of humoral immunity or may be persistently deficient in antibody production. To differentiate between these entities, we examined the 23-valent pneumococcal polysaccharide (PnPS) vaccine-induced IgM-, IgG- and IgA antibody responses in a cohort of 66 children with recurrent respiratory tract infections. Individual serum titres against 11 pneumococcal serotypes were measured by Luminex.