Tiger prowling: Distribution modelling for northward-expanding Aedes albopictus (Diptera: Culicidae) in Japan.

The Asian tiger mosquito, Aedes albopictus, is a significant public health concern owing to its expanding habitat and vector competence. Disease outbreaks attributed to this species have been reported in areas under its invasion, and its northward expansion in Japan has caused concern because of the potential for dengue virus infection in newly populated areas. Accurate prediction of Ae.

Pathological examination of Ym1, a chitinase family protein, in Mesocestoides corti-infected mice.

Mammals express a set of chitinase family proteins, comprising chitinases, which can hydrolyze chitin, and chitinase-like proteins without the chitinase activity but possessing chitin-binding properties. They act as endogenous lectins, regulating various physiological/pathological events. Ym1, originally identified as an eosinophil chemotactic factor or a macrophage-derived protein in parasite-infected mice, is a rodent-specific chitinase-like protein.

Identification of an eosinophil chemotactic factor from anopheline mosquitoes as a chitinase family protein.

Anopheline mosquitoes play an essential role in malaria transmission. The mosquito salivates copiously when probing for the location of a blood vessel. We found that the saliva of anopheline mosquitoes has chemotactic activity for naive eosinophils or neutrophils.

Schistosoma mekongi: a prominent neutrophil chemotactic activity of egg antigen with reference to that of Schistosoma japonicum.

Schistosoma mekongi causes granulomatous lesions around eggs deposited in the liver with neutrophil-rich inflammatory reactions in the early stage of the egg laying. To define the aspects of the typical pathogenesis of S. mekongi infection, we determined the difference between soluble egg antigen (SEA) from S.

Cellular expression of murine Ym1 and Ym2, chitinase family proteins, as revealed by in situ hybridization and immunohistochemistry.

Ym is one of the chitinase family proteins, which are widely distributed in mammalian bodies and can bind glycosaminoglycans such as heparin/heparan sulfate. Ym1 is a macrophage protein produced in parasitic infections, while its isoform, Ym2, is upregulated in lung under allergic conditions. In the present study, we revealed the distinct cellular expression of Ym1 and Ym2 in normal mice by in situ hybridization and immunohistochemistry.