Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P50583 (asymmetrical)
 12,197 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Low pH-induced binding of the bromelain-solubilized form of influenza virus hemagglutinin (BHA) to membranes occurs through the fusion peptide. From asymmetric hydrophobic photolabeling of membranes, evidence was obtained that this peptide penetrates only one leaflet of the bilayer. The asymmetrical labeling was achieved by employing a photoreactive analogue of a fatty acid whose transbilayer distribution can be manipulated by a membrane proton gradient.
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PMID:Testing topological models for the membrane penetration of the fusion peptide of influenza virus hemagglutinin. 258 83

Polarization of plasma membrane domains is an essential feature of secretory epithelial cells from exocrine glands. The surface of exocrine cells (a typical example is the acinar cell of the pancreas) is separated into an apical domain, where secretion occurs by exocytosis, and a basolateral domain, which senses variations of the internal milieu and is enriched with receptors for various hormones and secretagogues. It is unknown whether secretion is polarized in endocrine cells (except for thyroid follicular cells, which are organized into cavitary structures). To determine whether distinct plasma membrane domains exist in endocrine cells, we infected monolayer cultures of pancreatic endocrine cells with enveloped RNA viruses known to bud selectively from either the apical or basolateral domain in polarized epithelial cells. This asymmetrical budding is thought to reflect the polarized nature of the infected cells, as in non-polarized cells such as fibroblasts, the same viruses bud nonselectively from the entire cell surface. We show here that influenza virus and vesicular stomatitis virus (VSV) emerge asymmetrically from cultured pancreatic islet cells; this represents the first evidence for polarization of plasma membrane domains in pancreatic endocrine cells.
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PMID:Evidence for polarization of plasma membrane domains in pancreatic endocrine cells. 298 18

Growth characteristics of a wide range of influenza A viruses from different mammals and bird species were examined in an established line of canine kidney (MDCK) cells at an ordinary (37 degrees C) and a high temperature (42 degrees C). Although all viruses employed in the present study possessed a capability of replicating at 37 degrees C, virus growth at 42 degrees C showed considerable variation and reflected differences in the natural hosts of the isolates. All reference strains and isolates from bird species grew well in the MDCK cells maintained at 42 degrees C, but human viruses did not, showing an asymmetrical growth behavior. In contrast to this, growth of swine and equine viruses showed growth characteristics intermediate between human and avian viruses. Of the two swine viruses examined, replication of one strain occurred equally well at both temperatures and another failed to grow at 42 degrees C. Similarly, two of the three equine viruses tested belonging to H3N8 antigenic subtypes grew at 42 degrees C. However, the results obtained from comparison of plaque sizes and growth curves indicated that the replication of the above swine and equine viruses was restricted under a stringent temperature when compared to avian viruses. The detailed analysis of cloned viruses revealed that some of the swine and equine viruses contained two variants which are readily distinguished by growth behavior at 42 degrees C. Genome analysis of parental and virus clones by oligonucleotide mapping and migration profiles of RNA segments did not detect any differences among the above variants exhibiting the asymmetrical growth characteristics at 42 degrees C.
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PMID:Difference in growth behavior of human, swine, equine, and avian influenza viruses at a high temperature. 340 Nov 17

"Monospecific" antisera to the "fragile" hemaglutinnis of H0N1 (PR8) and H1N1 (FM1) influenza viruses detected an asymmetrical cross-reaction between these two strains that could not be explained by a common neuraminidase.
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PMID:Serological cross-reactions between the hemagglutinin subunits of H0N1 and H1N1 influenza viruses detected with "monospecific" antisera. 463 Jul 97

The influenza B virus protein, NB, was expressed in Escherichia coli, either with a C-terminal polyhistidine tag or with NB fused to the C-terminus of glutathione S-transferase (GST), and purified by affinity chromatography. NB produced ion channel activity when added to artificial lipid bilayers separating NaCl solutions with unequal concentrations (150-500 mM cis, 50 mM trans). An antibody to a peptide mimicking the 25 residues at the C-terminal end of NB, and amantadine at high concentration (2-3 mM), both depressed ion channel activity. Ion channels had a variable conductance, the lowest conductance observed being approximately 10 picosiemens. At a pH of 5.5 to 6.5, currents reversed at positive potentials indicating that the channel was more permeable to sodium than to chloride ions (PNa/PCl approximately 9). In asymmetrical NaCl solutions at a pH of 2.5, currents reversed closer to the chloride than to the sodium equilibrium potential indicating that the channel had become more permeable to chloride than to sodium ions (PCl/PNa approximately 4). It was concluded that, at normal pHs, NB forms cation-selective channels.
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PMID:Ion channels formed by NB, an influenza B virus protein. 866 76

Purified M2 protein from the Udorn strain of influenza virus was reconstituted into planar lipid bilayers from liposomes. In 1 mM HCl, the single-channel conductance was measured as 6 pS with open probability of < or =0.03. The current voltage curve is linear over the achievable voltage range. The current amplitude is amantadine sensitive. In HCl solutions, the single-channel current was essentially invariant with changes in [Cl(-)], [Na(+)], and [tetraethylammonium] ([TEA(+)]), but dependent on [H(+)]. The reversal potential, determined with asymmetrical hydrogen chloride solution, is very close to the equilibrium potential of hydrogen. This appears to be the first report of single-channel proton currents with the full-length M2 protein.
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PMID:Proton conductance of influenza virus M2 protein in planar lipid bilayers. 1534 48

Human parvovirus B19 infection in adults features clinical symptoms and laboratory abnormal findings unlike those in children commonly associated with cheek rash. We diagnosed 15 adult cases based on the positive increase in anti-parvovirus B19 IgM antibody (8.89 +/- 7.86 mean +/- SD, enzyme immunoassay (EIA)). Antibody titer was measured in 78 patients clinically showing fever, edema, exanthema, arthralgia, and myalgia among 11,040 outpatients first visiting the hospital from January 2005 to December 2007. Based on clinical and laboratory findings for these 15 cases, we recommended that physicians taking anti-parvovirus B19 antibody blood samples note whether (1) the level of C reactive protein is negative or low and without leucocytosis; (2) a miliary rash is observed in short duration (rarely facial); (3) arthralgia and/or myalgia is present in the extremities (sometimes asymmetrical); (4) edema is present in the extremities, especially finger, ankle, or sole of the foot; (5) contact has been made with ill children; (6) flu-like symptoms occur such as fatigue, headache, or fever;and (7) normo- or hypocomplementemia and/or antinuclear antibody is positive. Patients who fulfill requirement (1) plus at least three of requirements (2) through (7) should have a blood sample taken. We retrospectively studied 78 cases using these requirements, finding their sensitivity to be 100% (15/15), specificity to be 88.9% (56/63), positive predictive value to be 68.1% (15/22) and negative predictive value to be 100% (56/56). These requirements are thus useful in selecting patients for measuring antibody titer and definitively diagnosing severe or persistent parvovirus B19 infection occationally observed in adults.
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PMID:[Human parvovirus B19 infection in 15 adults--two-year Toho University Hospital study]. 1922 24

Plants survive against myriad environmental odds while remaining rooted to a single spot. The time scale over which plant cells can respond to environmental cues is seldom appreciated. Fluorescent protein-assisted live imaging of peroxisomes reveals that they respond within seconds of exposure to hydrogen peroxide and hydroxyl radicals by producing dynamic extensions called peroxules. Observations of the Arabidopsis flu mutant and treatments with xenobiotics eliciting singlet oxygen and superoxide reactive oxygen species suggest that the observed responses are specific for hydroxyl radicals. Prolonged exposure to hydroxyl radicals inhibits peroxule extension, and instead causes motile and spherical peroxisomes in a cell to become immotile and elongate several-fold. Expression of photo-convertible EosFP-PTS1 demonstrates that vermiform peroxisomes result from rapid stretching of individual peroxisomes, while the subsequent 'beads-on-a-string' morphology results from differential protein distribution within an elongated tubule. Over time, the beads in elongated peroxisomes also extend peroxules randomly before undergoing asynchronous, asymmetrical fission. Peroxule extension does not appear to involve cytoskeletal elements directly, but is closely aligned with and reflects the dynamics of ER tubules. Peroxisomal responses reveal a rapidly invoked subcellular machinery that is involved in recognition of hydroxyl stress thresholds, and its possible remediation locally through extension of peroxules or globally by increasing peroxisome numbers. A matrix protein retro-flow mechanism that supports peroxisome-ER connectivity in plant cells is suggested.
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PMID:Peroxule extension over ER-defined paths constitutes a rapid subcellular response to hydroxyl stress. 1982 Mar 26

The molecular architectures of enveloped viruses are one demonstrative example of perfectly arranged macromolecular complex that is achieved through the structural specificity of virus assembly. Virus morphogenesis is a multi-step process that depends on the concerted actions of many viral and cellular components as well as fitted organization of main viral constituents. Viral envelope was shown to be composed of the mixture of lipid raft and non-raft domains. The domains are recruited from the host-cell membrane as discrete well-ordered lipid-protein units in the process of virus assembly. Raft-like nature of influenza virus A envelope was visualized using a novel approach of cold solubilization of the detergent-resistant membranes from intact influenza virus A virions with the mixture of two non-ionic detergents drastically differing in their raft-solubilizing activities, NP40 and octyl-glucopyranoside. In the view of this methodological approach, the virus envelope is apparently an ensemble of platforms which are flexibly joint in the viral envelope, and composed of surface glycoproteins (hemagglutinin and neuraminidase), matrix M1 protein and lipids. The modern concept of transmembrane asymmetry of lateral domains in biological membranes was involved to explain the solubilization mechanism revealed. Using principles of this concept we suggest matrix M1 protein shell as a structure-forming base to support asymmetrical rafts in the virus envelope.
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PMID:[The concept of transmembrane asymmetry of lateral domains in biomemranes and influenza virus envelope fine structure]. 1980 18

A systematic, efficient means of producing diverse libraries of asymmetrically branched N-glycans is needed to investigate the specificities and biology of glycan-binding proteins. To that end, we describe a core pentasaccharide that at potential branching positions is modified by orthogonal protecting groups to allow selective attachment of specific saccharide moieties by chemical glycosylation. The appendages were selected so that the antenna of the resulting deprotected compounds could be selectively extended by glycosyltransferases to give libraries of asymmetrical multi-antennary glycans. The power of the methodology was demonstrated by the preparation of a series of complex oligosaccharides that were printed as microarrays and screened for binding to lectins and influenza-virus hemagglutinins, which showed that recognition is modulated by presentation of minimal epitopes in the context of complex N-glycans.
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PMID:A general strategy for the chemoenzymatic synthesis of asymmetrically branched N-glycans. 2416 73


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