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The effect of phospholipase A2 on mitochondrial glycerol-3-phosphate oxidation.

Glycerol-3-phosphate oxidation in brown adipose tissue mitochondria of cold-adapted hamster is strongly inhibited by phospholipase A2 (PLA2). Our data show that the glycerol-3-phosphate branch of the respiratory chain is sensitive to PLA2 action more than the succinate branch and that the transfer of reducing equivalents from the glycerol-3-phosphate dehydrogenase to artificial electron acceptor is especially sensitive to the PLA2 action.

Animals↗

Enhancement of Sia-lb1 antigenicity by sulphur-containing substituents at C-5 of free N-acetylneuraminic acid.

The Sia-lb1 epitope, recognized by anti-Sia-lb1 cold agglutinins, is unique since it is represented by the alpha-N-acetylneuraminic acid (alpha NeuNAc) monosaccharide. Chemical modifications of the chain at C-5 of alpha NeuNAc have shown that the natural 2-carbon and the artificial 3-carbon chains are optimal for anti-Sia-lb1 binding. Sia-lb1 antigenicity of alpha NeuNAc could be tenfold enhanced by replacement of the carbonyl oxygen by sulphur. The structural requirements of the Sia-lb1 epitope for optimal antibody binding were identified.

Agglutinins↗

Genome-wide transcriptional profiling of the Bacillus subtilis cold-shock response.

The transcriptome of Bacillus subtilis was analysed at different time points (30, 60 and 90 min) after a temperature downshift from 37 to 18 degrees C using DNA macroarrays. This approach allowed the identification of around 50 genes exhibiting an increased mRNA level and around 50 genes exhibiting a decreased mRNA level under cold-shock conditions. Many of the repressed genes encode enzymes involved in the biosynthesis of amino acids, nucleotides and coenzymes, indicating metabolic adaptation of the cells to the decreased growth rate at the lower temperature. The strongest cold-inducible gene encodes fatty acid desaturase, which forms unsaturated fatty acids from saturated phospholipid precursors, thereby increasing membrane fluidity. The cold-shock-induced increase of mRNA levels of the classical cold-shock genes cspB, cspC and cspD could be verified. Furthermore, besides many genes encoding proteins of unknown function, some genes encoding ribosomal proteins were transcriptionally up-regulated, which points to an adaptive reprogramming of the ribosomes under cold-shock conditions. Interestingly, the amount of mRNA specified by the operon ptb-bcd-buk-lpd-bkdA1-bkdA2-bkdB, which encodes enzymes involved in degradation of branched-chain amino acids, also increases after a temperature downshift. As cells utilize the isoleucine and valine degradation intermediates alpha-methylbutyryl-CoA and isobutyryl-CoA for synthesis of branched-chain fatty acids, this finding reflects the adaptation of membrane lipid composition, ensuring the maintenance of appropriate membrane fluidity at low temperatures. The results of the DNA array analyses were verified for several selected genes by RNA slot-blot analysis and compared with two-dimensional PAGE analyses.

Bacillus subtilis↗

Conformational and aggregational states of omega-aminoacylmelittin derivatives.

Melittin, a 26-residue peptide from bee venom, is known to change from a largely random to a largely alpha-helical conformation as a function of peptide concentration, pH, and ionic strength. In this report, we have determined the effect of displacing the positive charges of the amino groups of N-terminal glycine and lysine residues away from the backbone of melittin in coil-to-helix transitions by using omega-aminoacyl derivatives of melittin. These were prepared by acylating the amino groups of melittin with omega-amino acids to yield the melittin derivatives glycylmelittin (MLT-2), (4-aminobutanoyl)melittin (MLT-4), and (5-aminopentanoyl)melittin (MLT-5), respectively. At pH 7.2, there is a chain-length-dependent increase in helicity from MLT to MLT-5. The omega-aminoacylmelittin derivatives also show a concentration-dependent increase in helicity at pH 7.2. However, at pH 2.3, a concentration-independent, but chain length-dependent increase in helicity was observed. A hydrophilic derivative glycylglycylmelittin (MLT-GG) and a hydrophobic derivative MLT-5, which have side chains of equal length, show similar helicity, at pH 7.2, but at pH 2.3 MLT-GG shows almost no helicity, while MLT-5 is about 60% helical. The lysyl derivative (MLT-K), which has additional positive charges compared to melittin, behaves much like MLT-2. At pH 7.2, all the derivatives exhibit both cold- and heat-induced denaturation; a significant amount of residual structure is retained in the temperature range 80-100 degrees C. These results are discussed in terms of the electrostatic and hydrophobic interactions involving the side chains.

Amino Acid Sequence↗

Detection of human herpesvirus 6 DNA in throat swabs by polymerase chain reaction.

The detection of human herpesvirus 6 (HHV-6) DNA was carried out in throat swabs of adults and children by the polymerase chain reaction, and isolation of virus was also attempted from peripheral mononuclear cells. Although virus was isolated only from peripheral blood mononuclear cells of infants with exanthem subitum, HHV-6 DNA was detected in one of 30 healthy adults (3%), two of nine adults (22%) with common cold, two of 10 infants (20%) with exanthem subitum, four of 39 febrile children (10%) with antibody to HHV-6 (including three of 10 infants aged under 1 year old, and one of 29 children aged over 1 year old). However, HHV-6 DNA was not detected in samples from healthy neonates.

Adult↗

Multiple sclerosis attacks are associated with picornavirus infections.

Multiple sclerosis (MS) is a chronic demyelinating disease of the central nervous system, which often follows a relapsing-remitting (RR) course with discrete attacks. MS attacks have been associated with upper respiratory infections (URIs), but the specific viruses responsible have not been identified. We studied a cohort of 16 RRMS patients experiencing URI and followed them for clinically identifiable attacks. The viral causes of 21 separate URIs were investigated using culture and polymerase chain reaction (PCR) of nasal swab specimens, and by serology. Sibleys 'at-risk' period for MS attacks, beginning two weeks before and continuing for five weeks after a URI, was used for the analysis. Seven of the nine (78%) URIs due to picornaviruses were associated with an MS attack during the at-risk period. By contrast, only two of 12 (17%) picornavirus-negative URIs were associated with an MS attack (P = 0.01). The possible role of picornaviruses in the pathogenesis of MS deserves further study.

Adult↗

The association between respiratory viruses and symptoms in 2-week-old infants at high risk for asthma and allergy.

OBJECTIVES: The role of viral respiratory tract infections in the onset of childhood asthma and allergy is controversial, partly because of limited understanding about postnatal viral exposures. We investigated the prevalence of 3 common respiratory viruses and associated respiratory symptoms in 2-week-old infants at high risk for having asthma and allergy. STUDY DESIGN: Frozen nasal specimens from 2-week-old children at high risk (n = 495) underwent reverse transcription-polymerase chain reaction (RT-PCR) for picornavirus-, parainfluenza-, and respiratory syncytial virus-specific nucleic acid. RT-PCR findings were related to respiratory symptoms (cold, cough, and wheeze) and to characteristics implicated with increased risk for asthma and allergy. RESULTS: Viral RT-PCR was positive in 199 (40.2%) of 495 specimens examined, with picornavirus and parainfluenza significantly associated with respiratory symptoms. Viral prevalence was significantly higher in children born during the winter and summer months. CONCLUSIONS: A high percentage (40.2%) of infants at high risk for asthma and allergy had been exposed to common respiratory viruses at 2 weeks of age. RT-PCR is a powerful diagnostic method that can be used in epidemiologic studies examining the role of viral respiratory tract infections in the pathogenesis of pediatric asthma and allergy.

Asthma↗

Cold resistance of the brain during hibernation. III. Evidence of a lipid adaptation.

The composition of membrane-bound lipids of brain from both warm-adapted and hibernating hamsters were different in the complex lipid fraction as well as their fatty acyl chains. During hibernation the content of cholesterol was less, but there were greater amounts of both the phosphatidylcholines and phosphatidylethanolamines. There were small but significant increases in monounsaturated fatty acids as well as arachidonic acid in all the glycerophosphatides of the hibernating hamster, whereas a decrease in isomyristic acid was o0served in the sphingomyelins. The most significant changes observed occurred in the fatty aldehyde composition of ethanolamine plasmalogen. A dramatic increase in oleyaldehyde was observed during hibernation. These changes in membrane-bound lipids may account for the cold-resistant properties of the brain during hibernation by retaining the fluid nature of the cell membrane.

Acclimatization↗

Chilling stress leads to increased cell membrane rigidity in roots of coffee (Coffea arabica L.) seedlings.

Tropical and sub-tropical higher plant species show marked growth inhibition when exposed to chilling temperatures. In root tip segments of coffee seedlings which were subjected for 6 days to temperatures of 10, 15, 20 and 25 degrees C, in darkness, we have detected an increased amount of malondialdehyde formed in the 10 degrees C treatment, accompanied by higher electrolyte leakage. The electron paramagnetic resonance (EPR) technique and the fatty acid spin probes 5-, 12- and 16-doxylstearic acid were used to assess cellular membrane fluidity. At the depth of the 5th and 16th carbon atom of the alkyl chains the nitroxide radical detected more rigid membranes in seedlings subjected to 10 degrees C compared with 15 and 25 degrees C. At the C-12 position of the chains the probe showed very restricted motion and was insensitive to chilling induced membrane alterations. EPR parameters for intact tissues and microsome preparations from root tips showed that the fluidity was essentially the same when evaluated at C-5 and C-16 positions of the chains, and was considerably more fluid for microsomal membranes in the region of the C-12 position of the bilayers. The rotational motion of the nitroxide at C-16 position of the chains experienced a phase transition at about 15 degrees C. The calculated energy barriers for reorientational motion of the probe 16-doxylstearic acid were higher at temperatures of 5-15 degrees C than in the interval of 15-25 degrees C, suggesting that below the phase transition the membrane lipids assume a more ordered and compacted array. Membrane rigidity induced by chilling was interpreted as due to lipid peroxidation that could have been facilitated by higher density of peroxidizable chains below the membrane phase transition.

Coffee↗

Human antilipid A monoclonal antibodies bind to human B cells and the i antigen on cord red blood cells.

We describe two independently derived human mAb, A6(H4C5) and 216, initially selected for their reactivity to the lipid A domain of bacterial LPS, which also react with the following Ag: the i Ag present on cord RBC, a ligand on human B lymphocytes, and to certain autoantigens, defining these mAb as polyreactive. Both mAb have specific affinity for a carbohydrate epitope consisting minimally of a disaccharide with an acyl substitution at the 2-carbon position. Structural examination of the diverse Ag recognized by the two antibodies reveals the presence of this carbohydrate structure required for antibody binding. A6(H4C5) and 216 are IgM in isotype, but differ in their L chain expression. Molecular analysis shows that both the mAb are encoded by a highly conserved VH4 gene, designated VH4-21. This gene encodes a number of autoantibodies, particularly cold agglutinins. Specific recognition of lipid A and of a carbohydrate epitope on B lymphocytes by the two human mAb suggests a dual function for the highly conserved VH4-21 gene in antibacterial response and in B cell development and regulation.

Agglutinins↗

Structure of the tetrameric form of human L-Xylulose reductase: probing the inhibitor-binding site with molecular modeling and site-directed mutagenesis.

L-Xylulose reductase (XR) is a member of the short-chain dehydrogenase/reductase (SDR) superfamily. In this study we report the structure of the biological tetramer of human XR in complex with NADP(+) and a competitive inhibitor solved at 2.3 A resolution. A single subunit of human XR is formed by a centrally positioned, seven-stranded, parallel beta-sheet surrounded on either side by two arrays of three alpha-helices. Two helices located away from the main body of the protein form the variable substrate-binding cleft, while the dinucleotide coenzyme-binding motif is formed by a classical Rossmann fold. The tetrameric structure of XR, which is held together via salt bridges formed by the guanidino group of Arg203 from one monomer and the carboxylate group of the C-terminal residue Cys244 from the neighboring monomer, explains the ability of human XR to prevent the cold inactivation seen in the rodent forms of the enzyme. The orientations of Arg203 and Cys244 are maintained by a network of hydrogen bonds and main-chain interactions of Gln137, Glu238, Phe241, and Trp242. These interactions are similar to those defining the quaternary structure of the closely related carbonyl reductase from mouse lung. Molecular modeling and site-directed mutagenesis identified the active site residues His146 and Trp191 as forming essential contacts with inhibitors of XR. These results could provide a structural basis in the design of potent and specific inhibitors for human XR.

Amino Acid Motifs↗

Pseudomonas, the dominant polycyclic aromatic hydrocarbon-degrading bacteria isolated from Antarctic soils and the role of large plasmids in horizontal gene transfer.

Twenty-two polycyclic aromatic hydrocarbon (PAH)-degrading bacterial strains were isolated from Antarctic soils with naphthalene or phenanthrene as a sole carbon source, while no degrader was obtained from an unpolluted sampling site. Phylogenetic analysis showed that all belonged to the genus Pseudomonas except one that was identified as the genus of Rahnella. Some of them were closely related to previously reported cold-tolerant species, while some were separated in deeply rooted branches and represent new strains. All these strains showed a high efficiency to degrade naphthalene at 4 degrees C, and some additionally degraded phenanthrene. Using degenerate primers and polymerase chain reaction (PCR) amplification, ndo gene encoding naphthalene dioxygenase (NDO) was detected from all the isolates. Phylogenetic analysis grouped these genes into two clusters which shared 94% similarity to each other, and showed about 97% similarity within a cluster. However, no obvious difference was observed with mesophilic ndo genes; this indicates that the host cell is pivotal in cold adaptation. In addition, the mismatch between 16S rRNA and NDO phylogenetic trees strongly indicates horizontal gene transfer among these isolates and may have happened in situ. Further, Southern hybridization and plasmid curing confirmed that ndo genes were located on a large self-transmissible plasmid, which can be transferred to a mesophilic strains. The transconjugants acquired the ability to utilize naphthalene and phenanthrene. Results of this article imply that Pseudomonas plays an important role in PAH biodegradation in Antarctic soils, and the related genes might be originally transferred from outside Antarctica and spread among indigenous species.

Antarctic Regions↗

Rapid genotyping of mutant mice using dried blood spots for polymerase chain reaction (PCR) analysis.

Spontaneous neurologic mutations in the mouse provide powerful tools for the study of mammalian central nervous system development. The study of mouse neurologic mutants has led to a better understanding of the complex mechanisms involved in the development of the nervous system. Because few of these mutations have been identified, molecular probes distinguishing heterozygotes from homozygotes are generally unavailable. Further, most neurologic mouse mutants breed poorly as homozygotes, making it necessary to breed heterozygotes and select homozygous mutant progeny based on phenotype. The requirement for heterozygous breeding and the lack of molecular markers specific for the mutation have hampered developmental studies because the underlying neurologic perturbations occur before the mutant mice can be identified by phenotype. The recent identification and chromosomal assignment of simple sequence repeats (SSRs), repetitive sequences of DNA found at a high density throughout the mouse genome, provide the tools for mapping mutations in the mouse and for subsequent genotyping of potential mutants prior to phenotype onset. The SSRs are useful because these markers are polymorphic (for review see Weber, J.L., Human DNA polymorphisms based on length variations in simple-sequence tandem repeats. In: K.E. Davies and S.M. Tilghman (Eds.), Genetic and Physical Mapping. Genome Analysis, Vol. I, Cold Spring Harbor Laboratory Press, Plainview, NY, 1990, pp. 159-181 [16]), that is, the size of the individual SSRs differs among strains of mice. Following polymerase chain reaction (PCR) amplification of an SSR and separation of PCR products by polyacrylamide gel electrophoresis, one can easily visualize differences in the size of the PCR product between mouse strains. Many mutations in the mouse arose spontaneously on inbred strains and were subsequently backcrossed onto a different strain. After many generations of congenic backcrosses, the only DNA retained from the original mutant strain is composed of the mutant gene and closely linked regions. Thus, it is possible to cross the mutant strain to a different mouse strain and map the mutation by correlating mutant phenotype to SSRs the same size as the original mutant strain. We have mapped the tottering (tg), Purkinje cell degeneration (pcd), and nervous (nr) mutations using SSRs in backcrossed mouse strains. The SSRs distinguishing mutant from normal strains can then be used to genotype potential mutant pups before the onset of the mutant phenotype. The protocol described below can be adapted to almost any mutation congenically inbred for genotyping. Here we describe a method for selecting primers appropriate for genotyping potential mouse mutants and a rapid protocol for genotype screening. Even with SSRs distinguishing mutant from normal mice, genotyping several mice simultaneously can be a daunting task. This is primarily because the protocols available for preparing DNA for PCR amplification are time-consuming, requiring several purification steps including phenol extractions. Although kits are commercially available for DNA preparation without organic extractions, these kits tend to be expensive. The protocol described is a rapid, inexpensive method of determining the genotype of mice using PCR analysis of dried blood spots. The protocol only requires PCR primers distinguishing among alleles and is therefore ideal for the rapid identification of potential mutants for those mouse mutations which have been mapped using microsatellite markers. The DNA preparation protocol may also be used in rapid screening of potential transgenic mice.

Animals↗

Effect of solutes on the cold-induced insolubility of monoclonal cryoimmunoglobulins.

The effects of a variety of compounds upon the cold-induced insolubility of the IgM-K cryoglobulin McE have been examined. Cryoprecipitation was found to be inhibited by certain neutral salts, ureas, amides, tetraalkylammonium salts, long chain sodium alkyl sulfates, sugars, and a number of other agents. Cryoprecipitation was enhanced by increasing the hydrophobicity of alcohols, ureas, amides, and tetraalkylammonium salts, as well as by low concentrations of many solutes. With the exception of the alkyl sulfates, inhibition was not accompanied by detectable changes in conformation of the cryoimmunoglobulin. These inhibitions and enhancements were also associated with changes in the temperature at which cryoprecipitation was initiated as well as the temperature at which a low temperature-induced conformation change occurs in the McE protein. The effects of solutes on McE are compared to results obtained with five other (two IgG, three IgM) cryoimmunoglobulins, and it is hypothesized that electrostatic and dispersion forces are primarily responsible for the cold insolubility of monoclonal cryoimmunoglobulins.

Alcohols↗

Isolation and functional characterization of the active light chain of activated human blood coagulation factor XI.

Human blood coagulation Factor XIa was reduced and alkylated under mild conditions. The mixture containing alkylated heavy and light chains was subjected to affinity chromatography on high Mr kininogen-Sepharose. Alkylation experiments using [14C]iodoacetamide showed that a single disulfide bridge between the light and heavy chains was broken to release the light chain. The alkylated light chain (Mr = 35,000) did not bind to high Mr kininogen-Sepharose while the heavy chain (Mr = 48,000), like Factors XI and XIa, bound with high affinity. The isolated light chain retained the specific amidolytic activity of native Factor XIa against the oligopeptide substrate, pyroGlu-Pro-Arg-p-nitroanilide. Km and kcat values for this substrate were 0.56 mM and 350 s-1 for both Factor XIa and its light chain, and the amidolytic assay was not affected by CaCl2. However, in clotting assays using Factor XI-deficient plasma in the presence of kaolin, the light chain was only 1% as active as native Factor XIa. Human coagulation Factor IX was purified and labeled with sodium [3H]borohydride on its carbohydrate moieties. When this radiolabeled Factor IX was mixed with Factor XIa, an excellent correlation was observed between the appearance of Factor IXa clotting activity and tritiated activation peptide that was soluble in cold trichloroacetic acid. Factor XIa in the presence of 5 mM CaCl2 activated 3H-Factor IX 600 times faster than Factor XIa in the presence of EDTA. In the absence of calcium, Factor XIa and its light chain were equally active in activating 3H-Factor IX. In contrast to Factor XIa, the light chain in this reaction was inhibited by calcium ions such that, in the presence of 5 mM CaCl2, Factor XIa was 2000 times more effective than its light chain. Neither phospholipid nor high Mr kininogen and kaolin affected the activity of Factor XIa or its light chain in the activation of 3H-Factor IX. These observations show that the light chain region of Factor XIa contains the entire enzymatic active site. The heavy chain region contains the high affinity binding site for high Mr kininogen. Furthermore the heavy chain region of Factor XIa plays a major role in the calcium-dependent mechanisms that contribute to the activation of Factor IX.

Acetamides↗

Comparative sequence and structure analysis reveal features of cold adaptation of an enzyme in the thermolysin family.

Knowledge about the structural features underlying cold adaptation is important for designing enzymes of different industrial relevance. Vibriolysin from Antarctic bacterium strain 643 (VAB) is at present the only enzyme of the thermolysin family from an organism that thrive in extremely cold climate. In this study comparative sequence-structure analysis and molecular dynamics (MD) simulations were used to reveal the molecular features of cold adaptation of VAB. Amino acid sequence analysis of 44 thermolysin enzymes showed that VAB compared to the other enzymes has: (1) fewer arginines, (2) a lower Arg/(Lys + Arg) ratio, (3) a lower fraction of large aliphatic side chains, expressed by the (Ile + Leu)/(Ile + Leu + Val) ratio, (4) more methionines, (5) more serines, and (6) more of the thermolabile amino acid asparagine. A model of the catalytic domain of VAB was constructed based on homology with pseudolysin. MD simulations for 3 ns of VAB, pseudolysin, and thermolysin supported the assumption that cold-adapted enzymes have a more flexible three-dimensional (3D) structure than their thermophilic and mesophilic counterparts, especially in some loop regions. The structural analysis indicated that VAB has fewer intramolecular cation-pi electron interactions and fewer hydrogen bonds than its mesophilic (pseudolysin) and thermophilic (thermolysin) counterparts. Lysine is the dominating cationic amino acids involved in salt bridges in VAB, while arginine is dominating in thermolysin and pseudolysin. VAB has a greater volume of inaccessible cavities than pseudolysin and thermolysin. The electrostatic potentials on the surface of the catalytic domain were also more negative for VAB than for thermolysin and pseudolysin. Thus, the MD simulations, the structural patterns, and the amino acid composition of VAB relative to other enzymes of the thermolysin family suggest that VAB possesses the biophysical properties generally following adaptation to cold climate.

Acclimatization↗