Plasmodium vivax Tryptophan-Rich Antigen PvTRAg33.5 Contains Alpha Helical Structure and Multidomain Architecture

Tryptophan-rich proteins from several malarial parasites have been identified where they play an important role in host-parasite interaction. Structural characterization of these proteins is needed to develop them as therapeutic targets. Here, we describe a novel Plasmodium vivax tryptophan-rich protein named PvTRAg33.5. It is expressed by blood stage(s) of the parasite and its gene contains two exons. The exon 1 encodes for a 23 amino acids long putative signal peptide which is likely to be cleaved off whereas the exon 2 encodes for the mature protein of 252 amino acids. The mature protein contains B-cell epitopes which were recognized by the human immune system during P.vivax infection. The PvTRAg33.5 contains 24 (9.5%) tryptophan residues and six motifs whose patterns were similar among tryptophan-rich proteins. The modeled structure of the PvTRAg33.5 consists of a multidomain architecture which is stabilized by the presence of large number of tryptophan residues. The recombinant PvTRAg33.5 showed predominantly α helical structure and alpha helix to beta sheet transition at pH below 4.5. Protein acquires an irreversible non-native state at temperature more than 50°C at neutral pH. Its secondary and tertiary structures remain stable in the presence of 35% alcohol but these structures are destabilized at higher alcohol concentrations due to the disturbance of hydrophobic interactions between tryptophanyl residues. These structural changes in the protein might occur during its translocation to interact with other proteins at its final destination for biological function such as erythrocyte invasion

Feeding habits and trophic morphology of inshore lizardfish (Synodus foetens) on the central continental shelf off Veracruz, Gulf of Mexico

The inshore lizardfish, Synodus foetens, is one of the most common coastal demersal predators on the continental shelf of the Gulf of Mexico (GOM), but the biology and feeding ecology of this species is virtually unknown. Between November 2001 and January 2003 (10 collections), 603 individuals of S. foetens ranging from 112 to 420 mm standard length (SL) and 13 to 630 g (wet weight) were collected from the continental shelf of Alvarado, Veracruz, Mexico. About 60% of the individuals had empty stomachs with the stomach fullness of the remaining individuals being distributed as follows: 5% full (24.8%), 50-75% full (13.5%), and completely full (1.7%). The mean (+/- SD) wet weight of stomach contents was 12.1 +/- 10.8 g during the rainy season, and 19.0 +/- 13.0 g during the nortes season. Seventeen prey items were identified, with the majority thereof being fish. The most important prey items were Upeneus parrus, Loligo pealei, Engyophrys senta, Trachurus lathami, and Anchoa hepsetus. Seasonal changes in the diet were observed, with U. parrus and L. pealei being the most important prey during the nortes season, whereas E. senta and L. pealei were the main items during the rainy season. Prey size selection was evident among size classes of S. foetens, although no trophic overlap was observed among size classes (C-lk \u3c= 0.004). High trophic level values were determined for all size classes by season (rainy season = 4.67, nortes season = 4.84), and indicated this species belongs to the piscivorous trophic guild that preys upon both demersal and pelagic species

High-Affinity Binding of Silybin Derivatives to the Nucleotide-Binding Domain of a Leishmania tropica P-Glycoprotein-Like Transporter and Chemosensitization of a Multidrug-Resistant Parasite to Daunomycin

In order to overcome the multidrug resistance mediated by P-glycoprotein-like transporters in Leishmania spp., we have studied the effects produced by derivatives of the flavanolignan silybin and related compounds lacking the monolignol unit on (i) the affinity of binding to a recombinant C-terminal nucleotide-binding domain of the L. tropica P-glycoprotein-like transporter and (ii) the sensitization to daunomycin on promastigote forms of a multidrug-resistant L. tropica line overexpressing the transporter. Oxidation of the flavanonol silybin to the corresponding flavonol dehydrosilybin, the presence of the monolignol unit, and the addition of a hydrophobic substituent such as dimethylallyl, especially at position 8 of ring A, considerably increased the binding affinity. The in vitro binding affinity of these compounds for the recombinant cytosolic domain correlated with their modulation of drug resistance phenotype. In particular, 8-(3,3-dimethylallyl)-dehydrosilybin effectively sensitized multidrug-resistant Leishmania spp. to daunomycin. The cytosolic domains are therefore attractive targets for the rational design of inhibitors against P-glycoprotein-like transporters