The members of an Epstein-Barr virus microRNA cluster cooperate to transform B lymphocytes.

Epstein-Barr virus (EBV) transforms B lymphocytes through the expression of the latent viral proteins EBNA and latent membrane protein (LMP). Recently, it has become apparent that microRNAs (miRNAs) also contribute to EBV's oncogenic properties; recombinant EBVs that lack the BHRF1 miRNA cluster display a reduced ability to transform B lymphocytes in vitro. Furthermore, infected cells evince a marked upregulation of the EBNA genes.

A viral microRNA cluster strongly potentiates the transforming properties of a human herpesvirus.

Epstein-Barr virus (EBV), an oncogenic human herpesvirus, induces cell proliferation after infection of resting B lymphocytes, its reservoir in vivo. The viral latent proteins are necessary for permanent B cell growth, but it is unknown whether they are sufficient. EBV was recently found to encode microRNAs (miRNAs) that are expressed in infected B cells and in some EBV-associated lymphomas.

The Epstein-Barr virus alkaline exonuclease BGLF5 serves pleiotropic functions in virus replication.

The Epstein-Barr virus (EBV) alkaline exonuclease BGLF5 has previously been recognized to contribute to immune evasion by downregulating production of HLA molecules during virus replication. We have constructed a BGLF5-null virus mutant to determine BGLF5's functions during EBV viral replication. Quantification of virus production in permissive 293 cells carrying a DeltaBGLF5 genome identified a 17- to 21-fold reduction relative to complemented or wild-type controls.

Partial substitution of NO(3)(-) by NH(4)(+) fertilization increases ammonium assimilating enzyme activities and reduces the deleterious effects of salinity on the growth of barley.

Productivity of cereal crops is restricted in saline soils but may be improved by nitrogen nutrition. In this study, the effect of ionic nitrogen form on growth, mineral content, protein content and ammonium assimilation enzyme activities of barley (Hordeum vulgare cv. Alexis L.

Activity and protein level of AO isoforms in pea plants (Pisum sativum L.) during vegetative development and in response to stress conditions.

Among three AO isoforms detected in pea plants, the activity of PAO-1 was dominant in leaves of seedlings and young leaves of mature plants, while PAO-3 revealed the highest band intensity in old leaves and roots. PAO-1 and PAO-3 are homodimers consisting of 145 kDa and 140 kDa subunits, respectively, while PAO-2 is a heterodimer of one 145 kDa and one 140 kDa subunit. In leaves, the activity of PAO-1 disappeared gradually with leaf ageing, while in roots it was present only in seedlings but not in mature pea plants.