Sphaceloma coryli: A Reemerging Pathogen Causing Heavy Losses on Hazelnut in Southern Italy.

In 2013 to 2014, a disease causing severe crop losses was observed in several growing areas of the Campania region in southern Italy. Disease symptoms consisted of necrotic spots on leaves, bracts, and shells along with vein necrosis. Nuts were necrotic or aborted and symptomatic fruit dropped prematurely. A fungus was consistently isolated from symptomatic tissues and morphologically identified as Sphaceloma coryli. The fungus was first reported in France and Italy (Campania) over 30 years ago and was not subsequently documented until 2006 in the Latium region of Italy. When artificially inoculated on healthy hazelnut plants, disease symptoms were reproduced. The teleomorph of S. coryli was recorded for the first time on overwintering tissues of hazelnut trees. It was also induced in vitro. The morphology of asci and ascospores together with phylogenetic analysis based on internal transcribed spacer sequences indicated that the teleomorph is an undescribed species within the genus Elsinoë for which the name of Elsinoë coryli is proposed. Optimum temperatures for ascospore and conidium germination and mycelium growth were determined in vitro. The inhibition effect of some commercial fungicides on S. coryli was also evaluated in vitro.

Characterisation of a specific phycocyanin-hydrolysing protease purified from Spirulina platensis.

A novel protease has been identified, purified and partially characterised from complete medium grown Spirulina platensis, which could be responsible for the selective proteolysis of phycobiliproteins. It is an 80 kDa homodimeric enzyme; its N-terminal sequence is not related to any known protease sequence. It hydrolyses native phycocyanins in both crude extracts and reconstructed systems with purified Allo- or C-phycocyanin. It is inactive on several native proteins, including ribulose-1,5-bisphosphate carboxylase. The two phycocyanins are degraded at different velocities since C-phycocyanin is the better substrate, in agreement with the earlier observations on the progress of the phycobilisome disassembly. Specificity for synthetic substrates and inhibitors strongly suggests its assignment to the serine-protease family. The enzyme, however, is insensitive to the commercially available protein inhibitors of trypsin-like proteases.

Aging, free radicals, and antioxidants in wheat seeds.

Free radical oxidative attack is considered a major cause of disruption and deteriorative changes observed in aged seeds. Antioxidant defense mechanisms may remove potentially damaging molecular species, and carotenoids may act as radical scavengers. The content of lutein, the major carotenoid in wheat seeds, was determined in the flours. It showed a rapid decrease during seed aging. In addition, the content of free radicals in glutens made from flours of wheat seeds after long-term storage was studied. The concentration of radicals appeared to be age dependent, because the highest content of radicals was detected between 13 and 15 years of aging over 36 years of storage. Specific spin labeling of the sulfhydryl groups of gluten proteins enabled comparative EPR studies of the rigidity of the protein chains. A progressive stiffening of polymeric gluten with seed storage was found.

Reversible binding of ethacrynic acid to human serum albumin: difference circular dichroism study.

The reversible binding of ethacrynic acid was characterized by a difference circular dichroism method. A 2/1 stoichiometry was determined for the [drug]/[HSA] (human serum albumin) complex. The reversible binding of ethacrynic acid to HSA determines direct competition with ligands that selectivity bind to site II and to the fatty acid site. Furthermore, indirect competition was shown for ligands for site I (anti-cooperative) and to site III (cooperative).

Chemical modification of human albumin at cys34 by ethacrynic acid: structural characterisation and binding properties.

Derivatization of the free cys3,4 in human albumin, which is reported to occur under physiological conditions, has been performed in vitro by reaction of the protein with ethacrynic acid. This modification has been investigated by mass spectrometry and circular dichroism. Ethacrynic acid has been proven to bind human albumin either covalently and non-covalently. This post-translational modification does not determine significant changes in the secondary structure of the protein, as shown by the comparable circular dichroism spectra of the native and the modified proteins. Furthermore, the binding properties of the human albumin samples have been investigated by circular dichroism and equilibrium dialysis. The affinity to the higher affinity binding sites does not change either for drugs binding to site I, like phenylbutazone, or to site II, like diazepam, while a small but significant increase has been observed for bilirubin, known to bind to site III. Nevertheless significant decreases of the affinity at the lower affinity binding sites of the modified protein were observed for both drugs binding to site I or to site II.