SEARCH · PubMed Health

Results for “cold adaptation”

Explore indexed PubMed citations for clinical trials, systematic reviews and public health research. Read source abstracts and follow each citation to its original PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 91 records · Page 5Linked to original sources

PubMed1982

Catecholamines and triiodothyronine variations and the calorigenic response to norepinephrine in cold-adapted and exercise-trained rats.

A comparison was made of the thermogenic response to norepinephrine (NE) in cold-adapted (2 h per day at -15 degrees C for 5 weeks) and in exercise-trained rats (2 h swimming per day for 5 weeks). The oxygen consumption and the plasma catecholamine elevation were comparable for both conditions. Similarly plasma corticosterone determinations indicated comparable elevations in acute stress exposure and reduced responses in both exercise-trained and cold-adapted rats. The marked increase in colonic temperature which was observed in cold-adapted animals injected with NE (30 micrograms/100 g s.c.) was not found in exercise-trained rats. Similarly the brown adipose tissue was double in size in the cold-adapted rats but remained unchanged with exercise training. An important elevation of triiodothyronine (T3) was found in cold-exposed rats, either adapted or not. However, exercise was found to decrease plasma T3 in trained and nontrained rats. The results indicate that swimming for 2 h and exposure to cold (-15 degrees C) for 2 h produced comparable elevation of plasma corticosterone and catecholamine, and of oxygen consumption. However, only the cold-adapted animals develop a NE-induced thermogenesis. It is suggested that thyroid hormones are necessary as permissive factor, in stress-induced thermogenesis.

Acclimatization↗

PubMedDate not supplied

[Live cold-adapted reassortant influenza vaccines].

The author reviews studies of live cold-adapted reassortant influenza vaccines developed in Russia and USA. These vaccines are safe and weakly reactogenic for all age groups. The vaccines (two immunizations) are highly effective in children of preschool and school age and far less effective in adults. For elderly subjects simultaneous vaccination with live and inactivated vaccines is recommended. The probability of influenza prevention by a single injection of cold-adapted vaccines is to be further investigated. Modern data indicate that cold-adapted reassortant influenza vaccines can be used for influenza prevention only in children of preschool and school age.

Adaptation, Biological↗

PubMed1998

Structures of the psychrophilic Alteromonas haloplanctis alpha-amylase give insights into cold adaptation at a molecular level.

BACKGROUND: . Enzymes from psychrophilic (cold-adapted) microorganisms operate at temperatures close to 0 degreesC, where the activity of their mesophilic and thermophilic counterparts is drastically reduced. It has generally been assumed that thermophily is associated with rigid proteins, whereas psychrophilic enzymes have a tendency to be more flexible. RESULTS: . Insights into the cold adaptation of proteins are gained on the basis of a psychrophilic protein's molecular structure. To this end, we have determined the structure of the recombinant form of a psychrophilic alpha-amylase from Alteromonas haloplanctis at 2.4 A resolution. We have compared this with the structure of the wild-type enzyme, recently solved at 2.0 A resolution, and with available structures of their mesophilic counterparts. These comparative studies have enabled us to identify possible determinants of cold adaptation. CONCLUSIONS: . We propose that an increased resilience of the molecular surface and a less rigid protein core, with less interdomain interactions, are determining factors of the conformational flexibility that allows efficient enzyme catalysis in cold environments.

Adaptation, Physiological↗

PubMed1999

Residue determinants and sequence analysis of cold-adapted trypsins.

The digestive enzyme trypsin is among the most extensively studied proteins, and its structure has been reported from a large number of organisms. This article focuses on the trypsins from vertebrates adapted to life at low temperatures. Cold-adapted organisms seem to have compensated for the reduced reaction rates at low temperatures by evolving more active and less temperature-stable enzymes. We have analyzed 27 trypsin sequences from a variety of organisms to find unique attributes for the cold-adapted trypsins, comparing trypsins from salmon, Antarctic fish, cod, and pufferfish to other vertebrate trypsins. Both the "cold" and the "warm" active trypsins have about 50 amino acids that are unique and conserved within each class. The main unique features of the cold-adapted trypsins attributable to low-temperature adaptation seem to be (1) reduced hydrophobicity and packing density of the core, mainly because of a lower (Ile + Leu)/(Ile + Leu + Val) ratio, (2) reduced stability of the C-terminal, (3) lack of one warm trypsin conserved proline residue and one proline tyrosine stacking, (4) difference in charge and flexibility of loops extending the binding pocket, and (5) different conformation of the "autolysis" loop that is likely to be involved in substrate binding.

Amino Acid Sequence↗

PubMedDate not supplied

[The effect of amplifying reproduction of influenza virus in mouse lungs during simultaneous infection with two cold-adapted strains].

Reproduction of cold-adapted (ca) strains of influenza virus in the lungs of white mice after separate and combined inoculation and the properties of isolates derived from the infected animals were studied. It was shown that after combined inoculation with ca and ts strains A/Leningrad/134/17/57 (H2N2) and A/PR/8/59/1 (H1N1) ca recombinants could develop loosing some ts mutations and possessing (unlike the master strains) pneumo-virulence for mice. All the pneumo-virulent reassortants inherited hemagglutinin from the ca A/PR/8/59/1 strain and PB1 protein from the ca A/Leningrad/134/17/57 strain. The results indicate that it is unsafe to construct live recombinant divaccines by combining the recombinants produced from different donors of attenuation.

Adaptation, Biological↗

PubMed1983

Modification of liver mitochondrial lipids and of adenine nucleotide translocase and oxidative phosphorylation by cold adaptation.

The decrease in respiration rate following thyroidectomy is preceded by changes in the lipid composition of the mitochondrial membrane (Hoch, F.L., Subramanian, C., Dhopeshwarkar, G.A. and Mead, J.F. (1981) Lipids 16, 328-334) and in concert, changes in the kinetic parameters of the adenine nucleotide translocase (Mak, I.T., Shrago, E. and Elson, C.E. (1981) Fed. Proc. 40, 398). To demonstrate that physiological adaptation also involves this sequence of events, rats were housed at 8 degrees C for 3-4 weeks. Cold adaptation resulted in a modest (5%) increase in the unsaturation index for the mitochondrial fatty acids comprised of a significant increase in arachidonic acid and a reciprocal decrease in linoleic acid. Phospholipid analysis indicated that cold adaptation increased the mitochondrial phosphatidylethanolamine and reciprocally decreased the phosphatidylcholine content. Concomitantly, cold adaptation resulted in 25-30% increases in rat liver mitochondrial respiratory activities without changing the respiratory control or ADP/O ratios. The kinetic parameters of the adenine nucleotide translocase were determined by the back-exchange method (Pfaff, E. and Klingenberg, M. (1968) Eur. J. Biochem. 6, 66-79). At 0-4 and 10 degrees C, the Vmax and Km of the cold-adapted rat liver adenine nucleotide translocase were not distinguishable from the control values. The Ki values determined by Dixon plot studies for atractylate and palmitoyl-CoA were also comparable between the two groups. However, at 25 and 37 degrees C, cold-adapted rat liver adenine nucleotide translocase exhibited a 20% increase in Vmax and a 20% decrease in Km for external ADP. The results suggest that one adaption to a cold environment involves hormone-mediated changes in the lipid composition in the mitochondrial membranes which in turn modulate the adenine nucleotide translocase and subsequent respiratory activities.

Acclimatization↗

PubMed1987

Cold-adaptation of human rotavirus.

A human rotavirus strain was cold-adapted for possible future use as a live vaccine. The original strain was isolated in 1980 in primary cynomolgus monkey kidney cells and has a serotype I and subgroup II antigenicity. The virus was serially passaged in African green monkey kidney cells; it was cultivated at 37 degrees C at the first stage of passages, and the cultivation temperature was then shifted down stepwise by 3 degrees C per each 10 passages. Finally the virus was passaged 10 times at 25 degrees C (total passage number of 55). The virus formed small-size plaques with irregular shaped borders at 31 degrees C. Growth at 25 degrees C of the cold-adapted virus was higher than that of the original virus. There was no difference between the migration patterns of 11 dsRNA segments in polyacrylamide gel electrophoresis of the original and the cold-adapted viruses.

Adaptation, Physiological↗

PubMed1983

[Electrophysiological characteristics of muscle fibers in cold-adapted rats].

In rats, the membrane APs of single muscle fibers of fast (m. gastrocnemius) and slow (m. soleus) muscles were measured in cold--adapted animals and in a control group. In cold--adapted rats the membrane AP of slow muscle fibers was higher than in the control group, whereas in the fast muscle fibers the AP was decreased. The AP in cold--adapted rats fast muscle fibers was shorter and in the slow muscle fibers longer than in muscles of the control group. The data suggest that the excitation processes are changed in both types of muscles in cold--adapted rats.

Action Potentials↗

PubMedDate not supplied

[Cold-adapted strain of A/Leningrad/134/47/57 (H2N2)--a special attenuation donor of live influenza vaccine for children and the isolation of its recombinants].

A cold-adapted A/Leningrad/134/47/57 (H2N2) strain, a special donor of attenuation for generation of recombinant vaccine strains safe for children, has been developed and characterized. The genetic markers of this virus (temperature sensitivity of the cold-adapted strain, temperature optimum of the neuraminidase activity) were compared with those of A/Leningrad/134/17/57 (H2N2) strain, a donor of attenuation for a live influenza vaccine for adults. The A/Leningrad/134/47/57 (H2N2) strain was found to have a more marked temperature sensitivity and cold adaptation which correlated with the presence in its genome of multiple temperature-sensitive mutations in genes 1, 2, 5, 7, and 8. When the cold-adapted A/Leningrad/134/47/57 (H2N2) strain was hybridized with epidemic A/Brazil/11/78 (H1N1) and A/Bangkok/1/79 (H3N2) strains, recombinants were isolated which are candidate vaccine strains for a live influenza vaccine for children. The recombinants inherited the antigenic specificity of the current viruses and the temperature specificity and cold-adaptation of the donor of attenuation, A/Leningrad/134/47/57 (H2N2).

Adaptation, Physiological↗

PubMed2006

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↗

PubMed1990

Cold-adapted vaccine strains of influenza A virus act as dominant negative mutants in mixed infections with wild-type influenza A virus.

The cold-adapted reassortant of influenza A, which is a candidate live virus vaccine, interfered with the replication of parental wild-type virus in mixed infections of either MDCK cells or embryonated eggs. The interference occurred at either the permissive or nonpermissive temperature for the cold-adapted virus. In doubly infected cells, the yield of the wild-type virus was reduced by as much as 3000-fold and the protein synthesis phenotype expressed was that of the cold-adapted virus. The interference was detected even when infection with wild-type virus was carried out at a 9-fold excess or 2 hr before infection with the cold-adapted virus. As well as interfering with its wild-type parental virus, the cold-adapted virus also inhibited the replication of a heterologous influenza A subtype. In addition to its immunogenic potential, the ability to interfere with the replication of wild-type viruses is a desirable trait for any live, attenuated virus vaccine.

Animals↗

PubMed2004

Recombinant cold-adapted trypsin I from Atlantic cod-expression, purification, and identification.

Atlantic cod trypsin I is a cold-adapted proteolytic enzyme exhibiting approximately 20 times higher catalytic efficiency (kcat/KM) than its mesophilic bovine counterpart for the simple amide substrate BAPNA. In general, cold-adapted proteolytic enzymes are sensitive to autolytic degradation, thermal inactivation as well as molecular aggregation, even at temperatures as low as 18-25 degrees C which may explain the problems observed with their expression, activation, and purification. Prior to the data presented here, there have been no reports in the literature on the expression of psychrophilic or cold-adapted proteolytic enzymes from fish. Nevertheless, numerous cold-adapted proteolytic microbial enzymes have been successfully expressed in bacteria and yeast. This report describes successful expression, activation, and purification of the recombinant cod trypsin I in the His-Patch ThioFusion Escherichia coli expression system. The E. coli pThioHis expression vector used in the study enabled the formation of a fusion protein between a highly soluble fraction of HP-thioredoxin contained in the vector and the N-terminal end of the precursor form of cod trypsin I. The HP-thioredoxin part of the fusion protein binds to a metal-chelating ProBond column, which facilitated its purification. The cod trypsin I part of the purified fusion protein was released by proteolytic cleavage, resulting in concomitant activation of the recombinant enzyme. The recombinant cod trypsin I was purified to homogeneity on a trypsin-specific benzamidine affinity column. The identity of the recombinant enzyme was demonstrated by electrophoresis and chromatography.

Adaptation, Physiological↗

PubMed1990

[The characteristics of long-term dentate tetanus of the skeletal muscle in the rat after cold adaptation].

Prolonged unfused tetanuses of control and cold-adapted rats' m. gastrocnemius at different muscle temperature (29-30 and 24-25 degrees C) were studied. The time of achievement of the maximum level increased, the phase of higher thermogenesis became longer and the third economic phase was delayed after cold adaptation (both at 29-30 degrees C and 24-25 degrees C).

Adaptation, Physiological↗

PubMed1986

Study of live recombinant cold-adapted influenza bivalent vaccine of type A for use in children: an epidemiological control trial.

Live cold-adapted recombinant bivalent vaccine of influenza type A was studied in a controlled field trial in 1982-1983 among nearly 30,000 children 3-15 years old. The bivalent vaccine consisted of recombinants 47/25/1 (H1N1) and 47/7/2 (H3N2) of wild-type viruses A/Brazil/11/78 (H1N1) and A/Bangkok/1/79 (H3N2) with cold-adapted donor A/Leningrad/134/47/57 (H2N2). The recombinants which received mutant nonglycoprotein genes from cold-adapted donor did not suppress each other after simultaneous inoculation of children and stimulated antibody response to both strains. The bivalent vaccine was completely attenuated for children. It caused less than 1% transient febrile reactions during five days after the first vaccination, including double seronegative individuals with low antibody titres to both vaccinal strains. The cold-adapted bivalent vaccine tested proved to be safe for children according to the analysis of morbidity studies among vaccines and a control group performed during the five days and the following six months after the first immunization. There is a similar distribution of non-influenza illnesses and a statistically significant decrease in influenza-like diseases among vaccines compared to the control group. In the four months after the immunization programme was completed, epidemics of influenza A H1N1 and H3N2 occurred. The incidence of influenza-like diseases was approximately 50% less in the vaccinated than in the control groups. This is the first evidence of safety and protective efficacy of recombinant live influenza vaccine for children 3-15 years of age.

Adolescent↗

PubMed2005

Effects of neuropeptide Y antagonists on food intake in rats: differences with cold-adaptation.

Hyperphagia followed both central neuropeptide Y (NPY) administration and the presumed increase of endogenous NPY activity after food deprivation. NPY induced greater hyperphagia in cold-adapted than non-adapted rats; fasting of comparable severity caused similar hyperphagia in the two groups. NPY-receptor-antagonist D-Tyr(27,36), D-Thr32-NPY(27,36) or functional NPY-antagonist D-myo-inositol-1,2,6-trisphosphate attenuated the hyperphagic effect of both NPY and fasting in non-adapted rats. However, while completely preventing the NPY-hyperphagia, they did not influence the fasting-induced hyperphagia in cold-adapted rats. With cold-adaptation the sensitivity to NPY and to its antagonists increases, but the hypothalamic NPY loses from its fundamental role in the regulation of food intake, and the hyperphagia seen in cold-adaptation may need some other explanation.

Animals↗

PubMed1993

Evaluation of live attenuated cold-adapted influenza B/Yamagata/16/88 reassortant virus vaccine in healthy adults.

The safety and immunogenicity of a new cold-adapted reassortant influenza B/Yamagata/10/88 virus vaccine was evaluated in healthy young adults with low levels of preinoculation serum antibody to the vaccine virus, and symptoms and viral shedding after vaccination were compared with those following administration of the homologous B/Yamagata/88 wild-type virus. Administration of the cold-adapted virus was well tolerated and resulted in a significantly lower frequency of respiratory symptoms and viral shedding than did the wild-type virus. Twelve of 14 subjects who received the cold-adapted virus had an antibody response to the vaccine virus following vaccination. These data suggest that the B/Yamagata/88 virus is safe and immunogenic in seronegative adults and support the concept that the attenuation phenotype can be transferred reliably and reproducibly to successive new influenza B wild-type viruses along with the six internal gene segments of the cold-adapted influenza B/Ann Arbor/1/66 master vaccine virus.

Adaptation, Physiological↗

PubMed1990

Use of live cold-adapted influenza A H1N1 and H3N2 virus vaccines in seropositive adults.

To investigate the immunogenicity and protective efficacy of cold-adapted influenza vaccine in individuals with underlying immunity to influenza A virus, we administered cold-adapted H1N1 and H3N2 vaccines to adults with prevaccination serum hemagglutination inhibition antibody titers of 1:16 or more and challenged them 1 month afterwards with homologous wild-type influenza A virus. Both cold-adapted vaccines were immunogenic in seropositive adults. In addition, individuals receiving cold-adapted vaccines had lower rates of virus shedding and illness following challenge with wild-type influenza virus than did unvaccinated seropositive volunteers.

Administration, Intranasal↗

PubMed1978

Activation of the external pathway of NADH oxidation in liver mitochondria of cold-adapted rats.

15 min cold exposure of rats adapted to cold results in switching on a pathway of the fast oxidation of extramitochondrial NADH in the isolated liver mitochondria. This pathway is sensitive to mersalyl and cyanide, resistant to amytal and antimycin A, and can be stimulated by dinitrophenol. A portion of the endogenous cytochrome c pool can easily be removed by washing mitochondria of the cold-exposed rats. A scheme is discussed, postulating desorption of the inner membrane-bound cytochrome c into intermembrane space of mitochondria, resulting in formation of a link between the non-phosphorylating NADH-cytochrome c reductase in the outer mitochondrial membrane and cytochrome c oxidase in the inner membrane. It is suggested that such an oxidative pathway is involved in the urgent heat production in liver in response to the cold treatment.

Adaptation, Physiological↗