Taxonomic review of the genus Hypomicrogaster Ashmead (Hymenoptera: Braconidae: Microgastrinae), with descriptions of 40 new species.

A taxonomic review of the genus Hypomicrogaster Ashmead is presented with the redescription and redelimitation of the already named species Hypomicrogaster ecus Nixon, H. imitator (Ashmead), H. tydeus Nixon and H. zonaria (Say). The review also implies eleven new synonymies, and a new combination for the species H. areolaris (Blanchard). Also, the present revision identified 40 new Hypomicrogaster species: Hypomicrogaster aodous n. sp., H. aplebis n. sp., H. cernus n. sp., H. crocinus n. sp., H. daktulios n. sp., H. deltis n. sp., H. duo n. sp., H. epipagis n. sp., H. espera n. sp., H. evrys n. sp., H. guille n. sp., H. hektos n. sp., H. hupsos n. sp., H. ingensis n. sp., H. insolitus n. sp., H. inversalis n. sp., H. koinos n. sp., H. largus n. sp., H. laxus n. sp., H. linearis n. sp., H. lineatus n. sp., H. luisi n. sp., H. masoni n. sp., H. mesos n. sp., H. mikrosus n. sp., H. multus n. sp., H. pectinatus n. sp., H. plagios n. sp., H. pollex n. sp., H. rugosus n. sp., H. scindus n. sp., H. sicingens n. sp., H. sicpollex n. sp., H. sicscindus n. sp., H. siderion n. sp., H. spatulae n. sp., H. specialis n. sp., H. tantillus n. sp., H. tetra n. sp., H. zan n. sp. The Hypomicrogaster species are using as hosts 11 families of Lepidoptera, and 52 confirmed lepidopteran species feeding on 34 families of plants. Additionally, a fully illustrated key to all known described species of Hypomicrogaster is presented.

Crystallization, data collection and phasing of two digestive lysozymes from Musca domestica.

Lysozymes are mostly known for their defensive role against bacteria, but in several animals lysozymes have a digestive function. Here, the initial crystallographic characterization of two digestive lysozymes from Musca domestica are presented. The proteins were crystallized using the sitting-drop vapour-diffusion method in the presence of ammonium sulfate or PEG/2-propanol as the precipitant. X-ray diffraction data were collected to a maximum resolution of 1.9 angstroms using synchrotron radiation. The lysozyme 1 and 2 crystals belong to the monoclinic space group P2(1) (unit-cell parameters a = 36.52, b = 79.44, c = 45.20 angstroms, beta = 102.97 degrees) and the orthorhombic space group P2(1)2(1)2 (unit-cell parameters a = 73.90, b = 96.40, c = 33.27 angstroms), respectively. The crystal structures were solved by molecular replacement and structure refinement is in progress.

Purification and characterization of a phosphodiesterase from Bothrops alternatus snake venom.

A phosphodiesterase was purified from the venom of the snake Bothrops alternatus by a combination of gel filtration and ion exchange chromatographies. In SDS-PAGE, the enzyme gave a single band with a molecular mass of 105 kDa, which was unaltered in the presence of beta-mercaptoethanol, indicating that the protein contained no subunits. A single protein band was also observed in native PAGE. There were no contaminating 5'-nucleotidase, alkaline phosphatase and protease activities. The enzyme was recognized by commercial bothropic antiserum and gave a single band in immunoblotting. The enzyme had a pH optimum in the range of 7.5-9.5 and the optimum temperature was 60 degrees C, with activity being rapidly lost within 1 min at > or = 70 degrees C. The Km of the enzyme was 2.69 mM. PDE activity was potentiated by cobalt and, to a lesser extent, by calcium, whereas copper, manganese, zinc, EDTA, and beta-mercaptoethanol were inhibitory. These properties show that this enzyme is very similar to that isolated from other snake venoms.

Rabbit antivenom efficacy against myotoxic and neurotoxic activities of Bothrops jararacussu venom and Bothropstoxin-I

Bothrops jararacussu venom and its major toxin bothropstoxin-I (BthTX-I) possess myotoxic and neurotoxic properties. The efficacy of a rabbit antivenom raised against B. jararacussu venom in the neutralization of physiological, biochemical, and morphological changes induced by the venom and its major toxin BthTX-I was studied in mouse isolated phrenic nerve-diaphragm (PND) and extensor digitorum longus (EDL) preparations. The times required for 50 per cent neuromuscular blockade in PND and EDL preparations for venom were 70ñ11.5 (S.E.M., n=5) min and 58ñ8 (n=16) (50 µ/mL), and for BthTX-I 31ñ6 (n=3) min and 30ñ3 (n=5) min (20 µg/mL), respectively. After 120 min incubation, creatine kinase (CK) concentrations in solution containing the EDL preparations were 3464ñ346 U/L after exposure to venom (50 µg/mL, n=5) and 3422ñ135 U/L to BthTX-I (20µg/mL, n=4), respectively. Rabbit antivenom dose-dependently neutralized venom and toxin-induced neuromuscular blockade in both preparations and effectively prevented venom and toxin-induced CK release from EDL. Histological analysis showed that rabbit antivenom neutralized morphological damage caused by B.jararacussu venom and BthTX-I in EDL preparations. these results indicate that rabbit antivenom effectively neutralized the biological activities of B.jararacussu venom and BthTX-I.