Oomycetes: Lagenidium giganteum.

Lagenidium giganteum is a facultative parasite of mosquito larvae that initiates infection by production of biflagellate zoospores that selectively recognize and attach to larval cuticle. Following penetration of the cuticle, the parasite proliferates within the host, killing it within 24-60 h. Under optimum conditions the mycelia differentiate to produce asexual and/or sexual reproductive structures that produce zoospores within hours (asexual stage) to amplify the initial infection, or remain dormant for days, months or years (sexual stage), until conditions are conducive to mosquito breeding and spore germination. Recycling following a single application has been documented for up to 8-10 years. Environmental conditions that reduce or eliminate zoospore production, including temperature extremes (less than 16 degrees C or greater than 32 degrees C) and moderate levels of salinity and organic load, preclude use of the parasite for operational mosquito control. Three formulations of L. giganteum have been registered with the USEPA. Widespread use of the parasite will be possible when yields of the sexual stage in liquid culture are increased by a factor of ca. 10(2).

A phosphorylation site in Bruton's tyrosine kinase selectively regulates B cell calcium signaling efficiency by altering phospholipase C-gamma activation.

Loss of function of Bruton's tyrosine kinase (Btk) causes X-linked agammaglobulinemia (XLA) in humans and X-linked immunodeficiency in mice (xid). By using MS analysis and phosphopeptide-specific antibodies, we identified a tyrosine phosphorylation site (Y617) near the carboxyl terminus of the Btk domain from Btk expressed in 293T as well as DT-40 cells. Y617 is conserved in all Tec family kinases except murine Tec. Replacement of Y617 with a negatively charged glutamic acid (E) suppressed Btk-mediated phospholipase Cgamma2 activation and calcium response in DT-40 cells, whereas Akt activation was not affected. The Btk Y617E mutant could partially restore conventional B cell development and proliferation in Btk(-)/Tec(-) mice but failed to rescue CD5(+) B-1 cell development and the TI-II immune response to 2,4,6,-trinitrophenyl-Ficoll. These data suggest that Y617 phosphorylation or a negative charge at this site may down-regulate the function of Btk by selectively suppressing the B cell calcium signaling pathway.