Revision of the Euthalia phemius complex (Lepidoptera: Nymphalidae) based on morphology and molecular analyses

Adults of the Euthalia phemius complex, which is composed of three South‐East Asian nymphalid species, Euthalia phemius, Euthalia ipona, and Euthalia euphemia, were genetically analysed by examining mitochondrial and nuclear genes. The E. phemius complex was also examined morphologically, with particular emphasis on wing markings and male genitalia. No significant differences amongst the three species in the complex were detected with respect to either genetic distance or genital morphology. We therefore conclude that the three currently recognized Euthalia species belong to a single species. Accordingly, E. ipona is synonymized with E. phemius. Euthalia euphemia is treated as a subspecies of E. phemius. Type specimens of all taxa and a synonymic list for the E. phemius complex are also given. In addition, we briefly discuss the evolution and biogeography of the species complex. © 2011 The Linnean Society of London, Zoological Journal of the Linnean Society, 2012, 164 , 304–327.     

Purification and Substrate Specificity of Two Cysteine Proteinases of Giardia lamblia

The proteinase activity present in homogenates of trophozoites of Giardia lamblia , active on azocasein and urea-denaturated hemoglobin, was separated into two different enzymes by a series of purification procedures. These procedures included gel filtration on Fractogel TSK HW-55 (F), organomercurial agarose affinity chromatography, and ion exchange chromatography on DEAE-cellulose. By chromatography on Sephadex G-100, two purified enzymes exhibited relative molecular weights of M_r= 95,000 and 35,000 ± 10%, respectively. On the basis of inhibition by thiol reagents and abrogation of this effect by dithiothreitol and cysteine, they were identified as cysteine proteinases. Proteinase I (M_r= 95,000) and proteinase II (M_r= 35,000) were active against the β-chain of insulin releasing characteristic fragments. However, differences in substrate specificities of the two enzymes could be observed by using synthetic peptides that represent sequences 1–6, 8–18, and 20–30 of the insulin β-chain. Furthermore, the synthetic tetrapeptides Arg-Gly-Phe-Phe, Arg-Gly-Leu-Hyp, and Arg-Arg-Phe-Phe were hydrolyzed by the two proteinases releasing Phe-Phe and Leu-Hyp, respectively. Compared with Arg-Gly-Phe-Phe, the rates of hydrolysis of Arg-Gly-Leu-Hyp and Arg-Arg-Phe-Phe at substrate concentrations of 1 mM were 91% and 63% (proteinase I) and 80% and 57% (proteinase II), respectively.     

Different predation efficiencies of trap‐building larvae of sympatric antlions and wormlions from the rainforest of Borneo

1. This study reports the discovery of sympatric populations of antlions (Neuroptera: Myrmeleontidae) and wormlions (Diptera: Vermileonidae) in a unique system of sandy microhabitats in the lowland rainforest of Borneo. The two species convergently evolved sit‐and‐wait predatory larvae, which construct pitfall traps to hunt insects. Despite similar specialised foraging strategies, the two species coexist in the competitive environment of small, isolated sandy patches in the rainforest, which begs the question: what biological characteristics allow their coexistence? 2. Based on larval morphology alone, it was predicted that antlions would build larger traps, which would allow them to efficiently hunt larger prey. Addressing this hypothesis, this study compared the volumes of traps constructed by the two species under field and laboratory conditions. A laboratory experiment compared their efficiency of capture of three ant species that differed in body size. 3. The results show that antlions constructed larger traps and captured prey more efficiently. The difference between the species could not be explained by trap size alone. The findings demonstrate that the overlap in resource use in these two species was low, and it is suggested that there is a separation in prey utility between them, allowing their coexistence in the space‐limited habitat of the tropical rainforest.