Fungal origin of PBV-group viruses isolated from Penicillium brevi-compactum]

Treatment of extracts from the disintegrated mycelium of Penicillium brevi-compactum with antisera against viruses PBV-1 and PBV-3 grown on bacteria results in a considerable decrease in the infectiveness of micellar preparations toward E. coli C. This is a specific reaction since treatment with a heterologic antiserum against phage T2 has no effect on the infectiveness of the micellar extracts. The kinetics of reassociation of DNA from PBV-3 and DNA from Penicillium brevi-compactum has shown that the value of Cot at half-reassociation of these DNAs is 13.3 times higher than the value of Cot at half-reassociation of DNA from PBV-3 and heterologic DNA from chicken embryos. As was found by calculations, DNA isolated from the fungal mycelium contains virus sequences at an amount of 3.7 virus genomes per cell. These data confirm the micellar origin of the viruses PBV-1 and PBV-3. The virus PBV-3 is supposed to be present in the cells in the form of prophage.     

Fungal biotechnology

Fungi are used in many industrial processes, such as the production of enzymes, vitamins, polysaccharides, polyhydric alcohols, pigments, lipids, and glycolipids. Some of these products are produced commercially while others are potentially valuable in biotechnology. Fungal secondary metabolites are extremely important to our health and nutrition and have tremendous economic impact. In addition to the multiple reaction sequences of fermentations, fungi are extremely useful in carrying out biotransformation processes. These are becoming essential to the fine-chemical industry in the production of single-isomer intermediates. Recombinant DNA technology, which includes yeasts and other fungi as hosts, has markedly increased markets for microbial enzymes. Molecular manipulations have been added to mutational techniques as a means of increasing titers and yields of microbial processes and in the discovery of new drugs. Today, fungal biology is a major participant in global industry. Moreover, the best is yet to come as genomes of additional species are sequenced at some level (cDNA, complete genomes, expressed sequence tags) and gene and protein arrays become available.     

Fungal glucoamylases

Fungi are employed to produce industrially important glucoamylases. Most glucoamylases are glycosylated. Glycosylation enhances the enzyme stability. Glucoamylases contain both starch binding and catalytic binding domains, the former being responsible for activity on raw (insoluble) starch. Proteases may act on this domain causing the enzyme to lose its activity on insoluble starch. Optimal activity is observed at pH 4.5 to 6.5 and 50 to 70 degrees C. Glucoamylases contain up to 7 sub-sites with highly varying affinity. They can be produced by different methods including submerged, solid state and semi-solid state fermentation processes.     

Fungal chromosomes

There are now four well-established methods to examine the chromosomes of filamentous fungi: mapping genes to linkage groups by recombination analyses, light-microscopic observation of chromosomes in meiotic divisions, electron-microscopic observation of the synaptonemal complexes between homologous chromosomes in prophase of meiosis, and separation of chromosomes as individual bands by pulsed field gel electrophoresis. These techniques and their contributions are described in brief with special reference toNeurospora. A fifth technique will be used more and more in characterizing chromosomes at the molecular level as DNA sequencing is completed for a limited number of the fungi. However, only the molecular studies of chromosome structures as they relate to centromeres, telomeres or nucleolus organizer regions are discussed, as is the potential usefulness of DNA sequencing to identify the junctions of chromosome rearrangements.     

Fungal carotenoids

The Botanical Review -     

Fungal pathogenicity

Successful penetration of living plant tissue by fungal pathogens is preceded by an exchange of signals between both organisms. Recent mutational approaches revealed the importance of cAMP-dependent signalling pathways for fungal development and virulence on their hosts.     

Fungal endocarditis

Recent advances in medicine have caused fungal endocarditis (FE) to be a more common disease entity. A list of fungi is expanding as potential pathogens in FE, with Candida species and Aspergillus species being the most common. The combination of valvular heart disease along with indwelling devices and antibiotic use are the major predisposing factors for yeast endocarditis, whereas the presence of immunosuppression along with valvulopathy predisposes for mold endocarditis. The expanding population of immunosuppresed patients and individuals with intravascular devices has led to increased incidence of FE. Better outcome of FE depends on fast and accurate diagnosis and subsequent treatment. Echocardiography the most valuable recent technique allowed for early diagnosis of FE and is probably responsible for the improved prognosis of patients with FE. Nonculture-based diagnostic tests may further improve the sensitivity, specificity, and rapidity of microbiologic diagnosis of FE. The availability of the newer triazoles and echinocandins, providing broad spectrum antifungal activities with favorable safety profile may assist in achieving cure and further improving the prognosis of this disease entity.     

Fungal glucoamylases

The purification and properties of glucoamylase (α-l,4-glucan glucohydrolase, EC 3.2.1.3) from different fungal sources have been compared. The studies on the conformation and activity of the native enzyme at a function of pH, temperature, substrate concentration and the effect of denaturants and on the role of carbohydrate moiety on structure and stability have been reviewed. The chemical modification of the active centre, binding kinetics of the substrate and active site and the mechanism of action have been summarized. They differ in their fine structure as revealed by their near ultra-violet circular dichroism spectra and contain 30–35 % α-helix, 24–36 %Β-structure and the rest aperiodic structure. The activity of the enzyme is very sensitive to the environment around aromatic aminoacid residues. The glucoamylases are glycoprotein in nature, differ in their content and nature of carbohydrate from different sources. The carbohydrate moiety plays an important role in stabilising the native conformation of the enzyme and is not involved in activity and antigenecity. At the active site of the enzyme, two tryptophan and two carboxyl (glutamate or aspartate) groups are present. It is likely that the histidine and tyrosine residues which are present away from the active site are involved in binding of the substrate. There seems to be seven subsites which are involved in binding of the substrate and the catalytic site is situated in between 1 and 2 subsites. In breaking of α-1,4-, α-1,3-, and α-l,6-bonds only one active centre is involved. Studies on the immobilization of either glucoamylase alone or as a part of a multienzyme system have been reviewed briefly