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In the title centrosymmetric mononuclear copper(II) complex, [Cu(C(8)H(7)BrNO(2))(2)], the Cu(II) atom, lying on an inversion centre, is four-coordinated in a trans-CuN(2)O(2) square-planar geometry by two phenolate O atoms and two oxime N atoms from two symmetry-related N,O-bidentate oxime-type ligands. Inter-molecular C-H⋯O hydrogen bonds link neighbouring mol-ecules into a one-dimensional supra-molecular structure with an R(2) (2)(14) ring motif. This structure is further stabilized by π-π stacking inter-actions between adjacent benzene rings [centroid-centroid distance = 3.862 (1) Å].

In the mol-ecule of the title compound, C(13)H(10)ClN(3)OS, the dihedral angles between the plane through the thio-urea group and the pyridine and benzene rings are 53.08 (3) and 87.12 (3)°, respectively. The mol-ecules are linked by inter-molecular N-H⋯N hydrogen-bonding inter-actions to form a supra-molecular chain structure along the a axis. An intra-mol-ecular N-H⋯O hydrogen bond is also present.

The asymmetric unit of the title compound, C(22)H(16)N(6)O(6)S(2)·2C(2)H(6)OS, consists of one half-mol-ecule of the centrosymmetric thiourea derivative and one molecule of dimethyl sulfoxide (DMSO). The carbonyl group forms an intra-molecular hydrogen bond with the NH group, creating a six-membered (C-N-C-N-H⋯O) ring. Two other N-H⋯O hydro-gen bonds link one mol-ecule of the thio-urea to two mol-ecules of DMSO.

C-type lectins participate in pathogen recognition and other defense responses in innate immunity as well as in cell-cell interactions. A new cDNA encoding a 335-residue polypeptide containing two tandem C-type lectin domains was cloned from the haemocytes of Helicoverpa armigera (Ha-lectin). Northern hybridizations revealed that the mRNA of Ha-lectin was expressed constitutively in haemocytes, and was up-regulated following injections of bacteria, yeast, or virus. Ha-lectin expression was also induced in the fat body when larvae were injected with bacteria, yeast or 20-hydroxyecdysone and a non-steroidal ecdysone agonist, RH-2485. The Ha-lectin was detected in granular haemocytes. The recombinant protein (rHa-lectin) expressed in Escherichia coli had hemagglutinating and sugar-binding activities. The native Ha-lectin protein was identified in haemocytes and plasma using a polyclonal antiserum raised against rHa-lectin by immunoblotting techniques. All together, our results suggest that the Ha-lectin gene is involved in innate immunity, and may also participate in the molting process.

Background: Larval molting and metamorphosis are important physiological processes in the life cycle of the holometabolous insect. We used suppression subtractive hybridization (SSH) to identify genes differentially expressed during larval molting and metamorphosis., Results: We performed SSH between tissues from a variety of developmental stages, including molting 5th and feeding 6th instar larvae, metamorphically committed and feeding 5th instar larvae, and feeding 5th instar and metamorphically committed larvae. One hundred expressed sequence tags (ESTs) were identified and included 73 putative genes with similarity to known genes, and 27 unknown ESTs. SSH results were further characterized by dot blot, Northern blot, and RT-PCR. The expression levels of eleven genes were found to change during larval molting or metamorphosis, suggesting a functional role during these processes., Conclusion: These results provide a new set of genes expressed specifically during larval molt or metamorphosis that are candidates for further studies into the regulatory mechanisms of those stage-specific genes during larval molt and metamorphosis.