Functional role of phenylacetic acid from metapleural gland secretions in controlling fungal pathogens in evolutionarily derived leaf-cutting ants

Fungus-farming ant colonies vary four to five orders of magnitude in size. They employ compounds from actinomycete bacteria and exocrine glands as antimicrobial agents. Atta colonies have millions of ants and are particularly relevant for understanding hygienic strategies as they have abandoned their ancestors'' prime dependence on antibiotic-based biological control in favour of using metapleural gland (MG) chemical secretions. Atta MGs are unique in synthesizing large quantities of phenylacetic acid (PAA), a known but little investigated antimicrobial agent. We show that particularly the smallest workers greatly reduce germination rates of Escovopsis and Metarhizium spores after actively applying PAA to experimental infection targets in garden fragments and transferring the spores to the ants'' infrabuccal cavities. In vitro assays further indicated that Escovopsis strains isolated from evolutionarily derived leaf-cutting ants are less sensitive to PAA than strains from phylogenetically more basal fungus-farming ants, consistent with the dynamics of an evolutionary arms race between virulence and control for Escovopsis, but not Metarhizium. Atta ants form larger colonies with more extreme caste differentiation relative to other attines, in societies characterized by an almost complete absence of reproductive conflicts. We hypothesize that these changes are associated with unique evolutionary innovations in chemical pest management that appear robust against selection pressure for resistance by specialized mycopathogens.     

Metazoan parasites of Engraulis ringens as tools for stock discrimination along the Chilean coast

The value of the metazoan parasites of the anchoveta Engraulis ringens as biological tags for stock discrimination is assessed. Three hundred and fifty-nine specimens, obtained from six landing ports in northern and central Chile (Arica, Antofagasta, Caldera, Coquimbo, Valparaiso and Talcahuano) covering a latitudinal gradient of c . 18°, were analysed. Six metazoan parasite species (three ectoparasites and three endoparasites) were obtained. A correspondence analysis suggested that anchoveta from northern and central Chile are comprised of two stocks. Identification of stocks was largely based on qualitative differences (absence in southern localities of the monogenean Pseudanthocotyloides heterocotyle , a parasite proper of engraulids, and the copepod Caligus sp.) and quantitative differences in the prevalence of infection for the remaining species. Inertia and mass value for the correspondence analysis supported the hypothesis of two stocks.     

Inhibition of dihydropyridine-sensitive calcium channels by the plant alkaloid ryanodine

At micromolar concentrations, ryanodine interacts with the dihydropyridine receptor of rabbit skeletal muscle transverse tubules. Ryanodine displaces specifically bound [3H]PN200-110 with an apparent inhibition constant of approx. 95 microM and inhibits dihydropyridine-sensitive calcium channels in the same preparation with an IC50 of approx. 45 microM. These concentrations of ryanodine are approximately three orders of magnitude higher than those required to saturate binding of the alkaloid to the ryanodine receptor of sarcoplasmic reticulum and to open the calcium release channel of sarcoplasmic reticulum (i.e. 20 nM (1988) J. Gen. Physiol. 92, 1-26). Thus at sufficiently high dose, ryanodine may affect SR as well as plasma membrane Ca permeabilities.     

Purification of amoebolytic substances from Bacillus licheniformis M-4

Three antibiotic peptides with amoebolytic activity have been purified from culture supernatants of Bacillus licheniformis M-4 (amoebicins m4-A, m4-B, and m4-C). They were hydrophilic peptides consisting of six different amino acids (Asp, Glu, Ser, Thr, Pro, Tyr). Their molecular weights ranged from 3,000 to 3,200. Purified amoebicins were active against human pathogenic and non-pathogenic strains of Naegleria. They also showed a broad antifungal spectrum, but a narrow antibacterial activity.Abbreviations (TFA) Trifluoroacetic acid     

Determination of the gene sequence and the molecular structure of the enterococcal peptide antibiotic AS-48.

The structural gene of the enterococcal peptide antibiotic AS-48 (as-48) has been identified and cloned by using two degenerate 17-mer DNA oligonucleotides on the basis of the amino acid sequences of two peptides obtained by digestion of the antibiotic with Glu-C endoproteinase. That as-48 gene codes for a 105-amino-acid prepeptide, giving rise to a 70-amino-acid mature protein. Comparative analysis demonstrated that the 16-amino-acid sequence of one of the AS-48 Glu-C peptides, designated V8-5, was composed of a 12-amino-acid sequence corresponding to the C-terminal end sequence (from isoleucine +59 to tryptophan +70 [I+59 to W+70]) of the prepeptide and terminated in four residues forming the N terminus (M+1 to E+4) of a putative AS-48 propeptide. These data, combined with the characteristics of the gene sequence, strongly suggested that the antibiotic peptide was a 70-residue cyclic molecule. We propose that the AS-48 translated primary product is very likely submitted to a posttranslational modification during secretion (i) by an atypical or a typical signal peptidase that cleaves off a 35-residue or shorter signal peptide, respectively, from the prepeptide molecule and (ii) by the linkage of the methionine residue (M+1) to the C-terminal tryptophan residue (W+70) to obtain the cyclic peptide (a tail-head linkage).     

Gross (mesoscopic) and applied anatomy of the anterior inferior cerebellar artery in man with special reference to its course through the cerebellopontine angle region.

In the present paper, we describe anatomical variants of the anterior inferior cerebellar artery in man for applicative purposes. Our goal was to provide the surgeon with a detailed anatomical view of the region. This is similar to what he may observe through the surgical microscope using modern microsurgical techniques. We have focused our attention on the segments of the artery comprising its origin, its course until it reaches the cerebellum and its main collateral branches. Our results confirm the great variability of the elements under study, but enable the establishment of a few basic variational patterns. These patterns together with their relative frequency may be helpful in microsurgery.     

Ferralterin: An iron-sulfur protein functional in enzyme regulation in photosynthesis

The chloroplast new protein factor that was recently shown to link light to the activation of fructose 1,6-bisphosphatase was identified as a previously unrecognized iron-sulfur protein. This protein, given the name “ferralterin,” was purified to homogeneity from spinach leaves and from the blue-green alga (cyanobacterium) Nostoc muscorum. Ferralterin from both sources showed a visible absorption peak at 410nm, a molecular weight of about 30,000 and (provisionally) 4 g-atoms per mole each of nonheme iron and acid labile sulfide. The homogeneous ferralterin preparations catalyzed a light-dependent activation of chloroplast fructose 1,6-bisphosphatase that was dependent only on chlorophyll-containing membranes.     

Purification, characterization, and biological effects of a second bacteriocin from Enterococcus faecalis ssp. liquefaciens S-48 and its mutant strain B-48-28.

Enterococcus faecalis ssp. liquefaciens S-48 (producer of the peptide antibiotic AS-48) and its mutant B-48-28 (AS-48-) secrete the bacteriocin Bc-48. This substance has been purified to homogeneity from culture supernatants of strain B-48-28; it consists of a protein (80 kDa) stable from pH. 5.5 to 9.0 and sensitive to temperatures above 45 degrees C and to proteases. Its inhibitory spectrum is restricted to strains of Enterococcus faecalis. Bc-48 inhibits protein synthesis but does not affect amino acid uptake. A partial reduction of cell viability, together with autolysis, is also observed. Bc-48 differs from peptide AS-48 in both its molecular properties and mode of action.     

Genetic stability of the antagonistic character ofEnterococcus faecalis ssp.liquefaciens and the detection of a new inhibitory bacteriocin-like substance

The inhibitory capacity of strain S-48 ofEnterococcus faecalis ssp.liquefaciens was studied. The strain produces a broad-spectrum peptide antibiotic (AS-48) that has been characterized elsewhere. The isolation of mutants from S-48 after mutagenic treatment revealed another inhibitory substance which remained masked in the wild strain. The protein nature and restricted spectrum of this substance points to its being a bacteriocin (Bc-48).