Root surface phosphatase activity in ecotypes of Aegilops peregrina

The relationships between root surface phosphatase activity and the edaphic factors of their native habitats were investigated in four ecotypes of Aegilops peregrina (Hack.) Maire et Weil. In one set of experiments plants were grown in phosphate-deficient nutrient solution cultures (5 μ M ) with three pH values: 5.5, 6.5 and 7.5. In a second series, plants were grown in both P-poor and P-rich soils.
Results showed an optimal activity of the commonly-described root surface acid phosphatase of pH 4.5–5.0 in the ecotypes Meron (a P-poor montmorillonitic, typical mediterranean Terra-Rossa soil) and Har-Hurshan (a P-rich calcareous soil). However, in the ecotypes Malkiya (a P-rich kaolinitic Terra-Rossa) and Bet-Guvrin (a P-rich calcareous soil) the optimal activity of the phosphatase occurred at pH 6.0. The pH level of the growth solution had no effect on the pH of optimal activity of the phosphatase in the ecotypes Malkiya and Bet-Guvrin, but it somewhat affected their level of activity.
Phosphatase activity was stimulated when plant roots were grown in a P-poor soil, as compared to the activity of those which were grown in a P-rich soil. Plants of the Malkiya ecotype exhibited the strongest activation of phosphatase as compared to the other three ecotypes. It seems that ecotypes which have evolved in P-rich soils may regulate their root surface phosphatase activity better than those which have evolved in P-poor soils.     

Phenols in Cotton Seedlings Resistant and Susceptible to Alternaria macrospora

In healthy cotton seedlings, stems have a lower phenol content than leaves, but resistant plants have an altogether relatively higher phenol content than susceptible plants. Phenols extracted from infected plants can inhibit the growth of A. macrospora in vitro. In cotton plants infected with A. macrospora, phenols are oxidized by polyphenoloxidase rather than peroxidase and catalase. The main oxidative activity was around the developing necrotic area but activity was detected far from, necrosis as well. Though pre–inoculation mechanical injuries operated the phenol oxidation mechanism in the plant, they neither prevented nor encouraged the increase in disease severity. Isozyme pattern showed that contribution of all participants in the pathological interaction to the oxidative mechanism occurred in the diseased plant. A negative linear correlation was found between polyphenoloxidase activity, phenol accumulation and resistance. This study suggests that the phenol oxidative mechanism, participates in cotton plant resistance to A. macrospora.     

The Viral KSHV Chemokine vMIP-II Inhibits the Migration of Naive and Activated Human NK Cells by Antagonizing Two Distinct Chemokine Receptors

Natural killer (NK) cells are innate immune cells able to rapidly kill virus-infected and tumor cells. Two NK cell populations are found in the blood; the majority (90%) expresses the CD16 receptor and also express the CD56 protein in intermediate levels (CD56^Dim CD16^Pos) while the remaining 10% are CD16 negative and express CD56 in high levels (CD56^Bright CD16^Neg). NK cells also reside in some tissues and traffic to various infected organs through the usage of different chemokines and chemokine receptors. Kaposi''s sarcoma-associated herpesvirus (KSHV) is a human virus that has developed numerous sophisticated and versatile strategies to escape the attack of immune cells such as NK cells. Here, we investigate whether the KSHV derived cytokine (vIL-6) and chemokines (vMIP-I, vMIP-II, vMIP-III) affect NK cell activity. Using transwell migration assays, KSHV infected cells, as well as fusion and recombinant proteins, we show that out of the four cytokine/chemokines encoded by KSHV, vMIP-II is the only one that binds to the majority of NK cells, affecting their migration. We demonstrate that vMIP-II binds to two different receptors, CX3CR1 and CCR5, expressed by naïve CD56^Dim CD16^Pos NK cells and activated NK cells, respectively. Furthermore, we show that the binding of vMIP-II to CX3CR1 and CCR5 blocks the binding of the natural ligands of these receptors, Fractalkine (Fck) and RANTES, respectively. Finally, we show that vMIP-II inhibits the migration of naïve and activated NK cells towards Fck and RANTES. Thus, we present here a novel mechanism in which KSHV uses a unique protein that antagonizes the activity of two distinct chemokine receptors to inhibit the migration of naïve and activated NK cells.