A new role for PGRP-S (Tag7) in immune defense: lymphocyte migration is induced by a chemoattractant complex of Tag7 with Mts1

PGRP-S (Tag7) is an innate immunity protein involved in the antimicrobial defense systems, both in insects and in mammals. We have previously shown that Tag7 specifically interacts with several proteins, including Hsp70 and the calcium binding protein S100A4 (Mts1), providing a number of novel cellular functions. Here we show that Tag7–Mts1 complex causes chemotactic migration of lymphocytes, with NK cells being a preferred target. Cells of either innate immunity (neutrophils and monocytes) or acquired immunity (CD4⁺ and CD8⁺ lymphocytes) can produce this complex, which confirms the close connection between components of the 2 branches of immune response.     

Comparison of nucleotide sequences of ribosomal DNA of the mosquito genera Aedes and Ochlerotatus (Diptera: Culicidae: Aedini)

Morphological study allowed identifying 9 species of mosquitoes of the genus Ochlerotatus and 2 species of the genus Aedes. Sequencing of the rDNA region was performed for all these speciemens. The sequences of rDNA were the following: A. cinereus -868 bp, A. vexans--889 bp, Och. cantans--803 bp, O. excrucians--801 bp, O. euedes--794 bp, Och. cyprius--777 bp, O. diantaeus--758 bp, O. intrudens--817 bp, Och. punctor--783 bp, O. dorsalis--748 bp, O. species--767 bp. On average, the size of Aedes rDNA fragments exceeds rDNA of Ochlerotatus by 90-100 bp. The sequences are characterized by a high number of insertions and deletions, and also by point substitutions of nucleotides. It is important to notice that interspecific differences include not only different regions of the internal transcribed spacers, but also the conservative site which is represented by the 5.8S gene. Among four substitutions in this gene, one (C/A) represents the difference between Aedes and Ochlerotatus, the next (T/A) distinguishes A. cinereus from Ochlerotatus speciment and A. vexans, and two substitutions (A/C, T/G) testify the similarity between O. dorsalis and O. species and specimens of Aedes. Besides, two more deletions are typical for O. dorsalis and O. species. One deletion is com- mon, it distinguishes them from the other examined species, and another one is typical only for O. dorsalis. When analyzing morphological characteristics and comparing nucleotide rDNA sequences of O. species with the database, the similarity to O. caspius has been revealed. On the whole, phylogenetic relationships among Ochlerotatus species correspond to subdivision into groups based on morphological characters. Probably, examination of the larger number of specimens will change the morphological division into groups.     

AmylPepPred: Amyloidogenic Peptide Prediction tool

We present an efficient computational architecture designed using supervised machine learning model to predict amyloid fibril forming protein segments, named AmylPepPred. The proposed prediction model is based on bio-physio-chemical properties of primary sequences and auto-correlation function of their amino acid indices. AmylPepPred provides a user friendly web interface for the researchers to easily observe the fibril forming and non-fibril forming hexmers in a given protein sequence. We expect that this stratagem will be highly encouraging in discovering fibril forming regions in proteins thereby benefit in finding therapeutic agents that specifically aim these sequences for the inhibition and cure of amyloid illnesses.

Availability

AmylPepPred is available freely for academic use at www.zoommicro.in/amylpeppred     

The cyclooxygenases

Cyclooxygenases (COXs) catalyze the rate-limiting step in the production of prostaglandins, bioactive compounds involved in processes such as fever and sensitivity to pain, and are the target of aspirin-like drugs. COX genes have been cloned from coral, tunicates and vertebrates, and in all the phyla where they are found, there are two genes encoding two COX isoenzymes; it is unclear whether these genes arose from an early single duplication event or from multiple independent duplications in evolution. The intron-exon arrangement of COX genes is completely conserved in vertebrates and mostly conserved in all species. Exon boundaries largely define the four functional domains of the encoded protein: the amino-terminal hydrophobic signal peptide, the dimerization domain, the membrane-binding domain, and the catalytic domain. The catalytic domain of each enzyme contains distinct peroxidase and cyclooxygenase active sites; COXs are classified as members of the myeloperoxidase family. All COXs are homodimers and monotopic membrane proteins (inserted into only one leaflet of the membrane), and they appear to be targeted to the lumenal membrane of the endoplasmic reticulum, where they are N-glycosylated. In mammals, the two COX genes encode a constitutive isoenzyme (COX-1) and an inducible isoenzyme (COX-2); both are of significant pharmacological importance.     

'Navius' kissing stents for coronary bifurcation stenosis,recreating a new metallic carina: an IVUS-assessed case report

We report a case of implantation of a new design of stent which allows creation of a double-hemispheric lumen for the treatment of a bifurcational stenosis. The unfavourable outcome following the implantation of this stent is described.