RESUMO
We described immature stages of Nilio (Nilio ) brunneus Thomson, 1860 and provide a supplementary description for adults, including new data on the anatomy of the female and male terminalia. We observed N. brunneus feeding on the lichen Parmotrema sp., and that immature and adult are gregarious, with sessile pupae and generations overlapping. In laboratory, eggs hatched in 14 days and adults emerged after seven days in the pupal stage, the adults survived only a few days.(AU)
Assuntos
Animais , Tenebrio/anatomia & histologia , Tenebrio/classificação , Tenebrio/ultraestrutura , Tenebrio/crescimento & desenvolvimento , Líquens , Especificidade da EspécieRESUMO
We described immature stages of Nilio (Nilio ) brunneus Thomson, 1860 and provide a supplementary description for adults, including new data on the anatomy of the female and male terminalia. We observed N. brunneus feeding on the lichen Parmotrema sp., and that immature and adult are gregarious, with sessile pupae and generations overlapping. In laboratory, eggs hatched in 14 days and adults emerged after seven days in the pupal stage, the adults survived only a few days.
Assuntos
Animais , Tenebrio/anatomia & histologia , Tenebrio/classificação , Tenebrio/crescimento & desenvolvimento , Tenebrio/ultraestrutura , Especificidade da Espécie , LíquensRESUMO
The major beta-1,3-glucanase from Tenebrio molitor (TLam) was purified to homogeneity (yield, 6%; enrichment, 113 fold; specific activity, 4.4 U/mg). TLam has a molecular weight of 50 kDa and a pH optimum of 6. It is an endoglucanase that hydrolyzes beta-1,3-glucans as laminarin and yeast beta-1,3-1,6-glucan, but is inactive toward other polysaccharides (as unbranched beta-1,3-glucans or mixed beta-1,3-1,4-glucan from cereals) or disaccharides. The enzyme is not inhibited by high substrate concentrations and has low processivity (0.6). TLam has two ionizable groups involved in catalysis, and His, Tyr and Arg residues plus a divalent ion at the active site. A Cys residue important for TLam activity is exposed after laminarin binding. The cDNA coding for this enzyme was cloned and sequenced. It belongs to glycoside hydrolase family 16, and is related to other insect glucanases and glucan-binding proteins. Sequence analysis and homology modeling allowed the identification of some residues (E174, E179, H204, Y304, R127 and R181) at the active site of the enzyme, which may be important for TLam activity. TLam efficiently lyses fungal cells, suggesting a role in making available walls and cell contents to digestion and in protecting the midgut from pathogen infections.
Assuntos
Glucana Endo-1,3-beta-D-Glucosidase/genética , Glucana Endo-1,3-beta-D-Glucosidase/metabolismo , Tenebrio/enzimologia , Sequência de Aminoácidos , Animais , Sequência de Bases , Celulases/química , Celulases/metabolismo , Clonagem Molecular , Sequência Consenso , DNA Complementar/genética , DNA Complementar/metabolismo , Feminino , Trato Gastrointestinal/enzimologia , Regulação Enzimológica da Expressão Gênica , Glucana Endo-1,3-beta-D-Glucosidase/química , Concentração de Íons de Hidrogênio , Larva/enzimologia , Masculino , Modelos Moleculares , Dados de Sequência Molecular , Filogenia , Conformação Proteica , Alinhamento de Sequência , Tenebrio/classificação , Tenebrio/genéticaRESUMO
Duas espécies novas são acrescentadas ao gênero, anteriormente monotípico, Metoncidus Bates, 1871 (Carabidae, Loxandrini): M. epiphytus sp. nov. (localidade-tipo Peru: Loreto, Cocha Shinguito) e M. gracilus sp. nov. (localidade-tipo Peru: Tambopata, Madre de Dios). Informações que permitem a identificação do gênero dentre outros gêneros sul-americanos de carabídeos e uma chave para espécies de Mentocidus são fornecidas.