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PubMed1966

Operation WASP.

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Adolescent↗
PubMed2001

Spontaneous in vivo reversion of an inherited mutation in the Wiskott-Aldrich syndrome.

The Wiskott-Aldrich syndrome (WAS) is an X-linked primary immunodeficiency disease, arising from mutations of the WAS-protein (WASP) gene. Previously, we have reported that mononuclear cells from WAS patients showed lack/reduced of the intracellular WASP (WASP(dim)) by flow cytometric analysis, and analysis of WASP by flow cytometry (FCM-WASP) was useful for WAS diagnosis. In this study, we report a WAS patient who showed the unique pattern of FCM-WASP. The patient had the small population of normal expression of WASP (WASP(bright)) mononuclear cells together with the major WASP(dim) population. The WASP(bright) cells were detected in T cells, not in B cells or in monocytes. Surprisingly, the molecular studies of the WASP(bright) cells revealed that the inherited mutation of WASP gene was reversed to normal. His mother was proved as a WAS carrier, and HLA studies and microsatellite polymorphic studies proved that the WASP(bright) cells were derived from the patient himself. Therefore, we concluded that the WASP(bright) cells were resulted from spontaneous in vivo reversion of the inherited mutation. Furthermore, the scanning electron microscopic studies indicated that WASP-positive cells from the patient restored the dense microvillus surface projections that were hardly observed in the WASP(dim) cells. This case might have significant implications regarding the prospects of the future gene therapy for WAS patients.

Adult↗
PubMed1999

[The wasp/mosquito syndrome].

The authors describe for the first time the Wasp/Mosquito syndrome. The allergenic cross-reactivity between Vespula wasp venom and mosquito extract and the reverse rest objectively on several criteria. The frequency of the association between sensibilization to Vespula wasp venom and mosquito: In 10 subjects who had specific IgE to Vespula wasp venom 3 also had mosquito-specific IgE (30%), but out of 11 subjects with positive mosquito-specific IgE 10 also were positive with Vespula wasp venom specific IgE (about 91%). Three observations were documented showing a clinical and biological relationship between sensitisation to mosquito and wasp venom. A first patient had an anaphylactic reaction after a dozen mosquito bites. The allergy assessment confirmed sensitisation to the mosquitos, but also to Vespides (wasp, hornet) venoms. A second patient had an anaphylactic reaction after a wasp sting in 1997. From that date, he had local reactions, indeed loco-regional, to mosquito bites. The allergy assessment confirmed the double sensibilization to mosquito and wasp venom. Finally, a third patient at first had local reactions, also loco-regional, to mosquito bites, then two systemic reactions after mosquito bites. A first allergy assessment, made exclusively to hymenoptera venoms (not to mosquitos), showed a sensitivity to wasp venom and the patient, by mistake, was desensitised to wasp venom, which did not prevent recurrence after mosquito bites. After a second time, the allergy assessment for hymenoptera and mosquito, confirmed a double sensitisation (mosquito and Vespula wasp). Indirect criteria such as parallel increase in specific IgEs to Vespula wasp venom and mosquito in a patient who was desensitised only to mosquito and who had not been re-stung by wasps. Finally on direct criteria, such as: The inhibition technique by CAP RAST, which was positive in two ways: Vespula wasp--specific IgE was inhibited by mosquito extract, and vice versa. Electrophoresis, which showed a protein common to Vespula wasp venom and mosquito extract of M.W. of the order or 42KD and isoelectric point between 4.5 and 5. An immunoblot study identified this common protein with a M.W. of 44KD which is the same as hyaluronidase.

Adult↗
PubMed2002

Wiskott-Aldrich syndrome in a female.

Wiskott-Aldrich syndrome (WAS) is an X-linked disease characterized by thrombocytopenia, eczema, and various degrees of immune deficiency. Carriers of mutated WASP have nonrandom X chromosome inactivation in their blood cells and are disease-free. We report data on a 14-month-old girl with a history of WAS in her family who presented with thrombocytopenia, small platelets, and immunologic dysfunction. Sequencing of the WASP gene showed that the patient was heterozygous for the splice site mutation previously found in one of her relatives with WAS. Sequencing of all WASP exons revealed no other mutation. Levels of WASP in blood mononuclear cells were 60% of normal. Flow cytometry after intracellular staining of peripheral blood mononuclear cells with WASP monoclonal antibody revealed both WASP(bright) and WASP(dim) populations. X chromosome inactivation in the patient's blood cells was found to be random, demonstrating that both maternal and paternal active X chromosomes are present. These findings indicate that the female patient has a defect in the mechanisms that lead in disease-free WAS carriers to preferential survival/proliferation of cells bearing the active wild-type X chromosome. Whereas the patient's lymphocytes are skewed toward WASP(bright) cells, about 65% of her monocytes and the majority of her B cells (CD19(+)) are WASP(dim). Her naive T cells (CD3(+)CD45RA(+)) include WASP(bright) and WASP(dim) populations, but her memory T cells (CD3(+)CD45RA(-)) are all WASP(bright). After activation in vitro of T cells, all cells exhibited CD3(+)CD45RA(-) phenotype and most were WASP(bright) with active paternal (wild-type) X chromosome, suggesting selection against the mutated WASP allele during terminal T-cell maturation/differentiation.

Base Sequence↗
PubMed1998

Collagen induces tyrosine phosphorylation of Wiskott-Aldrich syndrome protein in human platelets.

Wiskott-Aldrich syndrome (WAS) and X-linked thrombocytopenia (XLT) are caused by mutations of the WAS protein (WASP) gene. All hematopoietic stem cell-derived lineages, including platelets, express WASP. Platelets from WAS patients are smaller than their normal counterparts and defects in platelet aggregation and actin polymerization have been reported. To determine if WASP is important for normal platelet function, we examined its role in signal transduction. We found that collagen but not thrombopoietin or thrombin induces a rapid and robust increase in tyrosine phosphorylation of platelet-associated WASP. Collagen-induced tyrosine phosphorylation of WASP was inhibited by cytochalasin D and wortmannin, respectively, suggesting that actin polymerization and phosphatidylinositol 3-kinase (PI3-kinase) play a role in the induction of tyrosine phosphorylation of WASP. Binding of glutathion S-transferase (GST)-Grb2 to WASP was seen in the lysate of resting platelets. The binding was reduced when lysates from collagen-stimulated platelets were incubated with GST-Grb2, suggesting that tyrosine phosphorylation of WASP may directly or indirectly modulate the adapter function of WASP. Although thrombin- and thrombopoietin-induced increase in tyrosine phosphorylation of WASP is negligible or marginal, WASP from thrombin-activated platelets became incorporated into the Triton X-100-insoluble 10, 000g sedimentable residue in an aggregation-dependent manner, suggesting that it may have a regulatory role in platelet cytoskeletal processes during aggregation. Lastly, we found that WASP is cleaved in response to activation of calpain, a protease that may have a role in postaggregation signaling processes. Our data suggest that collagen specifically induces an increase in tyrosine phosphorylation of WASP and that WASP is involved in signaling during thrombin-induced aggregation by its redistribution to the cytoskeleton and its cleavage during aggregation.

Adaptor Proteins, Signal Transducing↗