Genes of three naturally occurring monocot mannose-binding lectins from snowdrop (Galanthus nivalis L. agglutinin, GNA), garlic (Allium sativum L. leaf agglutinin, ASAL), and onion (Allium cepa L. agglutinin, ACA) and a recombinant fusion lectin between ASAL and ACA genes were expressed in a bacterial system. The pure and active form of the recombinant lectin peptides were utilized for estimation of their sensitivity potential against feeding nymphs of mustard aphid [Lipaphis erysimi (Kaltenbach)], a major sap-sucking insect pest of Indian mustard [Brassica juncea (L.) Czern.], an oilseed crop. The artificial diet bioassay revealed that ACA and the fusion lectin contained higher toxicity potential than GNA and ASAL. Ectopic expression of these lectins in mustard plants confirmed their protective capacity on the development of the population of aphids on transgenic plants. Based on the strong possibilities that lectins originating from diverse sources would have differential insecticidal potential against different insects, deployment of the appropriate lectin gene figures as crucial in the transgenic approach to protect crop plants against sapsucking insect pests.

Background: Fe-S cluster assembly in mitochondria involves generation of an activated form of sulfur called persulfide. Results: A novel experimental system tracks new Fe-S cluster synthesis in isolated mammalian mitochondria. Conclusion: The use of persulfide sulfur and iron for Fe-S cluster biogenesis is tightly coordinated by processes requiring GTP, NADH, and ATP. Significance: These cofactor targets can now be defined.

Prevotella intermedia is an oral bacterium implicated in a variety of oral diseases. Although internalization of this bacterium by nonphagocytic host cells is well established, the molecular players mediating the process are not well known. Here, the properties of a leucine-rich repeat (LRR) domain protein, designated AdpF, are described. This protein contains a leucine-rich region composed of 663 amino acid residues, and molecular modeling shows that it folds into a classical curved solenoid structure. The cell surface localization of recombinant AdpF (rAdpF) was confirmed by electron and confocal microscopy analyses. The recombinant form of this protein bound fibronectin in a dose-dependent manner. Furthermore, the protein was internalized by host cells, with the majority of the process accomplished within 30 min. The internalization of rAdpF was inhibited by nystatin, cytochalasin, latrunculin, nocodazole, and wortmannin, indicating that microtubules, microfilaments, and signal transduction are required for the invasion. It is noteworthy that preincubation of eukaryotic cells with AdpF increased P. intermedia 17 internalization by 5-and 10-fold for HeLa and NIH 3T3 fibroblast cell lines, respectively. The addition of the rAdpF protein was also very effective in inducing bacterial internalization into the oral epithelial cell line HN4, as well as into primary cells, including human oral keratinocytes (HOKs) and human umbilical vein endothelial cells (HUVECs). Finally, cells exposed to P. intermedia 17 internalized the bacteria more readily upon reinfection. Taken together, our data demonstrate that rAdpF plays a role in the internalization of P. intermedia 17 by a variety of host cells.