The role of antioxidant responses on the tolerance range of extreme halophyte Salsola crassa grown under toxic salt concentrations.

Salsola crassa (Amaranthaceae) is an annual halophytic species and naturally grows in arid soils that are toxic to most plants. In order to study the effects of salinity on their antioxidant system and to determine the tolerance range against salt stress, S. crassa seeds were grown with different concentrations of NaCl (0, 250, 500, 750, 1000, 1250 and 1500mM) for short (15d) and long-term (30d). Results showed that growth (RGR), water content (RWC) and osmotic potential (ΨΠ) decreased and, proline content (Pro) increased at prolonged salt treatment. Unlike K(+) and Ca(2+) contents, S. crassa highly accumulated Na(+) and Cl(-) contents. Chlorophyll fluorescence (Fv/Fm) only decreased in response to 1500mM NaCl at 30d. No salt stimulation of superoxide anion radical (O2(•-)) content was observed in plants treated with the range of 0-500mM NaCl during the experimental period. NaCl increased superoxide dismutase (SOD) activity depending on intensities of Mn-SOD and Fe-SOD isozymes except in 1500mM NaCl-treated plants at 30d. In contrast to catalase (CAT), peroxidase (POX) activity increased throughout the experiment. Also, salinity caused an increase in glutathione reductase (GR) and glutathione peroxidase (GPX) and decreased in ascorbate peroxidase (APX), monodehydroascorbate reductase (MDHAR) and dehydroascorbate reductase (DHAR) at 15d. Both total ascorbate (tAsA) and glutathione (tGlut) contents significantly increased in treated plants with 1000-1500mM NaCl at 15d. After 0-1000mM NaCl stress, H2O2 and TBARS contents were similar to control groups at 15d, which were consistent with the increased antioxidant activity (POX, GR and GPX). However, H2O2 content was more pronounced at 30d. Therefore, S. crassa exhibited inductions in lipid peroxidation (TBARS content) in response to extreme salt concentrations. These results suggest that S. crassa is tolerant to salt-induced damage at short-term treatments as well as extreme salt concentrations.

The acclimation of photosynthesis and respiration to temperature in the C3 -C4 intermediate Salsola divaricata: induction of high respiratory CO2 release under low temperature.

Photosynthesis in C(3) -C(4) intermediates reduces carbon loss by photorespiration through refixing photorespired CO(2) within bundle sheath cells. This is beneficial under warm temperatures where rates of photorespiration are high; however, it is unknown how photosynthesis in C(3) -C(4) plants acclimates to growth under cold conditions. Therefore, the cold tolerance of the C(3) -C(4) Salsola divaricata was tested to determine whether it reverts to C(3) photosynthesis when grown under low temperatures. Plants were grown under cold (15/10 °C), moderate (25/18 °C) or hot (35/25 °C) day/night temperatures and analysed to determine how photosynthesis, respiration and C(3) -C(4) features acclimate to these growth conditions. The CO(2) compensation point and net rates of CO(2) assimilation in cold-grown plants changed dramatically when measured in response to temperature. However, this was not due to the loss of C(3) -C(4) intermediacy, but rather to a large increase in mitochondrial respiration supported primarily by the non-phosphorylating alternative oxidative pathway (AOP) and, to a lesser degree, the cytochrome oxidative pathway (COP). The increase in respiration and AOP capacity in cold-grown plants likely protects against reactive oxygen species (ROS) in mitochondria and photodamage in chloroplasts by consuming excess reductant via the alternative mitochondrial respiratory electron transport chain.

Identification of methionine synthase (Sal k 3), as a novel allergen of Salsola kali pollen.

Salsola kali pollen is a common cause of pollinosis during summer and early fall in desert and semi-desert regions. The aim of this study was the identification and characterization of Sal k 3, a new allergen from S. kali pollen. S. kali pollen extract was fractionated by SDS-PAGE and the allergenic profile was determined by IgE-immunoblotting using twelve S. kali allergic patients. Protein identification was carried out by the means of mass spectrometry. Using degenerated primers, two DNA fragments encoding N- and C-terminal domain of Sal k 3 were amplified by PCR, then cloned into the PTZ57R/T vector and sequenced. The open reading frame of Sal k 3 fragments were subcloned in the pET-32b(+) vector, expressed in E. coli, and purified by Ni2+ affinity chromatography. The IgE-binding capacity of rSal k 3 fragments was then studied by IgE-immunoblotting, inhibition assays, and skin prick tests. A 45-kDa allergen was identified as a fragment of the cobalamin-independent methionine synthase (MetE) by mass spectrometry and was detected in the sera of 8/12 (66.6%) of S. kali allergic patients. Moreover, inhibition assays demonstrated that the purified rSal k 3 fragments were similar to their counterparts in the crude extract. Sal k 3 represents a new allergen of S. kali pollen and seems to be an important allergenic compound in S. kali pollen.

A pectin methylesterase as an allergenic marker for the sensitization to Russian thistle (Salsola kali) pollen.

BACKGROUND: Chenopodiaceae pollen is considered the main cause of pollen allergy in desert countries and its incidence is world-wide increasing by the desertization of extensive zones. Although the correlation between the sensitization to Chenopodium album and Salsola kali pollens of patients suffering from allergy to Chenopodiaceae pollens is high, a significant number of patients exhibited IgE sensitivity exclusively towards S. kali. OBJECTIVE: To analyse this differential reactivity and to purify, clone and characterize the putative responsible allergen. METHODS: Immunoblotting was used to analyse the IgE binding to pollen extract for S. kali and C. album. The protein was isolated by two chromatographic steps and characterized by Edman degradation, mass spectrometry, finger print analysis and Concanavalin A lectin staining. Specific cDNA was amplified by polymerase chain reaction, cloned in Escherichia coli and sequenced. Immunologic characterization was performed by immunoblotting, enzyme-linked immunoassay detection and inhibition experiments using sera from 11 patients allergic to S. kali pollen. RESULTS: cDNA codifies for a mature protein of 339 amino acids plus a putative signal peptide of 23 residues and it belongs to the plant pectin methylesterase (PME) family. It is a mildly basic and polymorphic protein and was recognized by the IgE from all the patients allergic to S. kali included in the study, and was called Sal k 1. The protein was not recognized in the C. album pollen extract using the sera of these patients. CONCLUSION: Sal k 1 is a protein from the PME family with a high allergenic relevance. Considering this allergen as responsible for the different sensitization between S. kali and C. album pollen, it may be a useful marker to classify patients allergic to Chenopodiaceae allowing a safer and more specific immunotherapy.