Minimum-Width Confidence Bands via Constraint Optimization

Peer reviewe

Биомаркеры фиброза трансплантированной почки

Fibrosis is one of the causes of kidney allograft loss, especially late after transplantation (up to 65% incidence after 2 years). The purpose of this literature review is to analyze studies examining noninvasive monitoring techniques for renal graft fibrosis.Фиброз является одной из причин потери аллотрансплантата почки, особенно в поздние сроки после трансплантации (частота встречаемости – до 65% через 2 года). Целью данного обзора литературы является анализ исследований, изучающих методы неинвазивного мониторинга развития фиброза почечного трансплантата

Functional characterization and biological significance of Yersinia pestis lipopolysaccharide biosynthesis genes

The Gram negative bacterium Yersinia pestis is the etiological agent of flea transmitted fulminant systemic rodent zoonosis and the reason of the three devastating pandemics of plague Lipopolysaccharide (LPS, endotoxin) is an impor tant factor of pathogenicity of Gram negative bacteria. The full LPS molecule (S form LPS) consists of three well defined domains: i) lipid A composed of sugars, fatty acids, and phosphate; it represents the endotoxic princi ple of the LPS and anchors it in the outer membrane; ii) a core oligosaccharide containing charged groups; and iii) an O specific polysaccharide (O antigen), which carries ISSN 0006 2979, Biochemistry (Moscow), 2011, Vol. 76, No. 7, pp. 808 822. © Pleiades Publishing, Ltd., 2011. Published in Russian in Biokhimiya, 2011, Vol. 76, No. 7, pp. 989 1005 Abstract-In silico analysis of available bacterial genomes revealed the phylogenetic proximity levels of enzymes responsible for biosynthesis of lipopolysaccharide (LPS) of Yersinia pestis, the cause of plague, to homologous proteins of closely relat ed Yersinia spp. and some other bacteria (Serratia proteamaculans, Erwinia carotovora, Burkholderia dolosa, Photorhabdus luminescens and others). Isogenic Y. pestis mutants with single or double mutations in 14 genes of LPS biosynthetic path ways were constructed by site directed mutagenesis on the base of the virulent strain 231 and its attenuated derivative. Using high resolution electrospray ionization mass spectrometry, the full LPS structures were elucidated in each mutant, and the sequence of monosaccharide transfers in the assembly of the LPS core was inferred. Truncation of the core decreased sig nificantly the resistance of bacteria to normal human serum and polymyxin B, the latter probably as a result of a less effi cient incorporation of 4 amino 4 deoxyarabinose into lipid A. Impairing of LPS biosynthesis resulted also in reduction of LPS dependent enzymatic activities of plasminogen activator and elevation of LD 50 and average survival time in mice and guinea pigs infected with experimental plague. Unraveling correlations between biological properties of bacteria and partic ular LPS structures may help a better understanding of pathogenesis of plague and implication of appropriate genes as potential molecular targets for treatment of plague

Developmental perspectives on interpersonal affective touch

In the last decade, philosophy, neuroscience and psychology alike have paid increasing attention to the study of interpersonal affective touch, which refers to the emotional and motivational facets of tactile sensation. Some aspects of affective touch have been linked to a neurophysiologically specialised system, namely the C tactile (CT) system. While the role of this sys-tem for affiliation, social bonding and communication of emotions have been widely investigated, only recently researchers have started to focus on the potential role of interpersonal affective touch in acquiring awareness of the body as our own, i.e. as belonging to our psychological ‘self’. We review and discuss recent developmental and adult findings, pointing to the central role of interpersonal affective touch in body awareness and social cognition in health and disorders. We propose that interpersonal affective touch, as an interoceptive modality invested of a social nature, can uniquely contribute to the ongoing debate in philosophy about the primacy of the relational nature of the minimal self

Evidence that WapB Is a 1,2-Glucosyltransferase of Pseudomonas aeruginosa Involved in Lipopolysaccharide Outer Core Biosynthesis▿†

Pseudomonas aeruginosa is an important opportunistic pathogen infecting debilitated individuals. One of the major virulence factors expressed by P. aeruginosa is lipopolysaccharide (LPS), which is composed of lipid A, core oligosaccharide (OS), and O-antigen polysaccharide. The core OS is divided into inner and outer regions. Although the structure of the outer core OS has been elucidated, the functions and mechanisms of the glycosyltransferases involved in core OS biogenesis are currently unknown. Here, we show that a previously uncharacterized gene, pa1014, is involved in outer core biosynthesis, and we propose to rename this gene wapB. We constructed a chromosomal mutant, wapB::Gm, in a PAO1 (O5 serotype) strain background. Characterization of the LPS from the mutant by Western immunoblotting showed a lack of reactivity to PAO1 outer core-specific monoclonal antibody (MAb) 5c-101. The chemical structure of the core OS of the wapB mutant was elucidated using nuclear magnetic resonance spectroscopy and mass spectrometry techniques and revealed that the core OS of the wapB mutant lacked the terminal β-1,2-linked-d-glucose residue. Complementation of the mutant with wapB in trans restored the core structure to one that is identical to that of the wild type. Eleven of the 20 P. aeruginosa International Antigenic Typing Scheme (IATS) serotypes produce LPSs that lack the terminal d-glucose residue (GlcIV). Interestingly, expressing wapB in each of these 11 serotypes modifies each of their outer core OS structures, which became reactive to MAb 5c-101 in Western immunoblotting, suggesting the presence of a terminal d-glucose in these core OS structures. Our results strongly suggested that wapB encodes a 1,2-glucosyltransferase