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PubMed2006

Microscopic rate-constants for substrate binding and acylation in cold-adaptation of trypsin I from Atlantic cod.

Temperature imposes limits on where life can thrive and this is evident in the evolution of the basic structural properties of proteins. Cold-adaptation of enzymes is one example, where the catalytic rate constant (k(cat)) is increased compared with hot-acclimated homologous under identical assay conditions. Trypsin I from Atlantic cod (Gadus morhua) has catalytic efficiency (k(cat)/K(m)) for amide hydrolysis that is 17-fold larger than observed for bovine trypsin. Here, the individual rate-constants for association of substrate (k(1)), dissociation of substrate (k(-1)), and acylation of the enzyme (k(2)) have been determined using benzoyl-Arg-p-nitroanilide or benzyloxycarbonyl-Gly-Pro-Arg-p-nitroanilide as substrates. Rather unexpectedly, by far the largest difference (37-fold increase) was observed in k(1), the rate constant for binding of substrate. The cold-adaptation of the dissociation and catalytic steps were not as prominent (increased by 3.7-fold). The length of substrate did have an effect by increasing the reaction rate by 70-fold, and again, the step most affected was the initial binding-step.

Acylation↗

PubMed1986

Immunity to influenza A virus infection in young children: a comparison of natural infection, live cold-adapted vaccine, and inactivated vaccine.

Live attenuated, cold-adapted (ca) influenza A vaccines administered intranasally have been well characterized as safe and immunogenic, but comparative data on protective efficacy are required for further development. In this study, 59 young children were divided into the following four groups based on prior exposure to influenza A (H3N2) virus: natural infection, live ca vaccine given intranasally, inactivated vaccine given im, and no previous exposure. Virus challenge with homologous live ca vaccine occurred 12 months after vaccination or natural infection. Prior natural infection and live ca vaccine significantly reduced ca virus shedding after challenge compared with inactivated vaccine or no prior exposure to influenza A virus. Prechallenge nasal IgA, detected almost exclusively in subjects naturally infected or vaccinated with live ca virus, was associated with protection. Although inactivated vaccine failed to produce significant local IgA during the primary response, it seemed to prime for secondary local antibody responses after challenge with live ca virus.

Administration, Intranasal↗

PubMed1977

Evidence that fatty acid synthesis in the interscapular brown adipose tissue of cold-adapted rats is increased in vivo by insulin by mechanisms involving parallel activation of pyruvate dehydrogenase and acetyl-coenzyme A carboxylase.

Plasma insulin concentrations in cold-adapted rats were altered acutely by administration of glucose or anti-insulin serum. Rates of fatty acid synthesis in interscapular brown adipose tissue were determined from the incorporation of 3H from 3H2O into tissue lipid. Rates of synthesis were greatly elevated after glucose administration and markedly decreased after injection with anti-insulin serum. Parallel changes in the initial activities of both acetyl-CoA carboxylase and pyruvate dehydrogenase were observed under these conditions, but no changes in total activities were evident. The results suggest that this tissue is an important site of fatty acid synthesis in the cold-adapted rat and that this feature of the tissue is sensitive to changes in plasma insulin concentrations.

Acetyl-CoA Carboxylase↗

PubMedDate not supplied

[Differentiating markers of virulent and attenuated (cold-adapted) strains of influenza A virus].

A high sensitivity of influenza virus to replication at a high temperature and a reduction of the temperature optimum of the neuraminidase activity are important genetic markers correlating with the degree of attenuation for the man. Cold-adapted variants of influenza virus produced in the course of passages at a low (25-28 degrees C) temperature are thermo-sensitive. The passage of the viruses at the optimal temperature (32 degrees C) does not change the range of thermal sensitivity even in variants, harmless for adult persons. The interfering activity of influenza viruses with different levels of human virulence was studied. A considerable portion of the examined cold-adapted strains differs from the original virulent strains in the capacity to interfere with the challenge virus in chick embryo fibroblast cell culture. However some thermosensitive variants as well as original strains do not react in interference tests. This indicates the lack of complete correlation between the interfering activity, thermal sensitivity and human virulence of influenza virus.

Adaptation, Physiological↗

PubMed1998

A cold-adapted lipase of an Alaskan psychrotroph, Pseudomonas sp. strain B11-1: gene cloning and enzyme purification and characterization.

A psychrotrophic bacterium producing a cold-adapted lipase upon growth at low temperatures was isolated from Alaskan soil and identified as a Pseudomonas strain. The lipase gene (lipP) was cloned from the strain and sequenced. The amino acid sequence deduced from the nucleotide sequence of the gene (924 bp) corresponded to a protein of 308 amino acid residues with a molecular weight of 33,714. LipP also has consensus motifs conserved in other cold-adapted lipases, i.e., Lipase 2 from Antarctic Moraxella TA144 (G. Feller, M. Thirty, J. L. Arpigny, and C. Gerday, DNA Cell Biol. 10:381-388, 1991) and the mammalian hormone-sensitive lipase (D. Langin, H. Laurell, L. S. Holst, P. Belfrage, and C. Holm, Proc. Natl. Acad. Sci. USA 90:4897-4901, 1993): a pentapeptide, GDSAG, containing the putative active-site serine and an HG dipeptide. LipP was purified from an extract of recombinant Escherichia coli C600 cells harboring a plasmid coding for the lipP gene. The enzyme showed a 1,3-positional specificity toward triolein. p-Nitrophenyl esters of fatty acids with short to medium chains (C4 and C6) served as good substrates. The enzyme was stable between pH 6 and 9, and the optimal pH for the enzymatic hydrolysis of tributyrin was around 8. The activation energies for the hydrolysis of p-nitrophenyl butyrate and p-nitrophenyl laurate were determined to be 11.2 and 7.7 kcal/mol, respectively, in the temperature range 5 to 35 degrees C. The enzyme was unstable at temperatures higher than 45 degrees C. The Km of the enzyme for p-nitrophenyl butyrate increased with increases in the assay temperature. The enzyme was strongly inhibited by Zn2+, Cu2+, Fe3+, and Hg2+ but was not affected by phenylmethylsulfonyl fluoride and bisnitrophenyl phosphate. Various water-miscible organic solvents, such as methanol and dimethyl sulfoxide, at concentrations of 0 to 30% (vol/vol) activated the enzyme.

Cloning, Molecular↗

PubMed1973

Comparative studies of wild-type and "cold-mutant" (temperature-sensitive) influenza viruses: polypeptide synthesis by an Asian (H2N2) strain and its cold-adapted variant.

The structure and replication of a cold-adapted, temperature-sensitive (TS) mutant of an Asian (H2N2) influenza virus was compared with that of its wild-type (WT) parent. Viruses were grown in a chicken kidney cell system, and at the nonpermissive temperature of 40 C, production of infectious TS virus was about 100,000-fold less than at 35 C, in contrast to WT virus. Major structural polypeptides of each virus grown at 35 C were similar, except that the hemagglutinin glycopolypeptide (HA) of the TS virions was slightly more heterogenous than that of WT virions. Synthesis of viral polypeptides was examined by sodium dodecyl sulfate acrylamide gel electrophoresis of pulse-labeled infected cells. This revealed a defect in the synthesis of TS viral hemagglutinin that was most pronounced at the nonpermissive temperature. Other TS viral polypeptides appeared to be synthesized normally at 40 C. A defect in the TS virus hemagglutinin was also indicated by serological studies that demonstrated that TS virus hemagglutinin had lost antigenic sites present on the WT virus. Thus, it is concluded that the virus mutant examined contains lesions in the hemagglutinin gene, although the possibility of additional unrecognized lesions is not excluded.

Adaptation, Biological↗

PubMed2005

[Identification of psychrotrophs SYP-A2-3 producing cold-adapted protease from the No. 1 Glacier of China and study on its fermentation conditions].

The psychrotrophs SYP-A2-3 producing the cold-adapted protease has been isolated from the bacterial samples collected from the No. 1 Glacier of China and identified as Bacillus cereus according to its morphological and physiochemical characteristics and 16s rDNA gene sequence analysis. It could grow between 0 degree C and 38 degrees C while its optimal growth temperature was 25 degrees C and the optimal temperature for its protease production was 15 degrees C. The cold-adapted protease was identified as neutral metallo-protease, the molecular weight was 34.2 kD shown by SDS-PAGE, the optimal pH and temperature for activity was 7.0-8.5 and 42 degrees C, respectively. Various fermentation conditions of its protease production were also investigated. The results showed that casein was the best nitrogen source while glucose and starch were suitable carbon source for its protease production. The initial pH of fermentation broth ranged from 6.5 to 7.0 was optimal. Under optimized conditions, the protease activity produced by SYP-A2-3 could reach 3800 U/mL and 4800 U/mL conducted in shaking flask and 5 L stirred jar experiment, respectively.

Bacillus cereus↗

PubMed2005

Influence of cooling temperature and duration on cold adaptation of Lactobacillus acidophilus RD758.

The effect of different cooling temperatures and durations on resistance to freezing and to frozen storage at -20 degrees C in Lactobacillus acidophilus RD758 was studied, by using a central composite rotatable design. A cold adaptation was observed when the cells were maintained at moderate temperature (26 degrees C) for a long time (8h) before being cooled to the final temperature of 15 degrees C. These conditions led to a low rate of loss in acidification activity during frozen storage (0.64 minday(-1)) and a high residual acidification activity after 180 days of frozen storage (1011 min). The experimental design allowed us to determine optimal cooling conditions, which were established at 28 degrees C during 8h. Adaptation to cold temperatures was related to an increase in the unsaturated to saturated fatty acid ratio and in the relative cycC19:0 fatty acid concentration. Moreover, an increased synthesis of four specific proteins was observed as an adaptive response to the optimal cooling conditions. They included the stress protein ATP-dependent ClpP and two cold induced proteins: pyruvate kinase and a putative glycoprotein endopeptidase.

Acclimatization↗

PubMed2006

Isolation and characterization of cold-adapted strains producing beta-galactosidase.

beta-Galactosidase is extensively employed in the manufacture of dairy products, including lactose-reduced milk. Here, we have isolated two gram-negative and rod-shaped coldadapted bacteria, BS 1 and HS 39. These strains were able to break down lactose at low temperatures. Although two isolates were found to grow well at 10 degrees , the BS 1 strain was unable to grow at 37 degrees . Another strain, HS-39, evidenced retarded growth at 37 degrees . The biochemical characteristics and the results of 16S rDNA sequencing identified the BS 1 isolate as Rahnella aquatilis, and showed that the HS 39 strain belonged to genus Buttiauxella. Whereas the R. aquatilis BS 1 strain generated maximal quantities of beta-galactosidase when incubated for 60 h at 10 degrees , Buttiauxella sp. HS-39 generated beta-galactosidase earlier, and at slightly lower levels, than R. aquatilis BS 1. The optimum temperature for beta-galactosidase was 30 degrees for R. aquatilis BS-1, and was 45 degrees for Buttiauxella sp. HS-39, thereby indicating that R. aquatilis BS-1 was able to generate a cold-adaptive enzyme. These two cold-adapted strains, and most notably the beta-galactosidase from each isolate, might prove useful in some biotechnological applications.

Cold Temperature↗

PubMed2003

Effect of yearly vaccinations with live, attenuated, cold-adapted, trivalent, intranasal influenza vaccines on antibody responses in children.

BACKGROUND: The cold-adapted, trivalent influenza vaccine (CAIV-T) may become an option for annual vaccination. However, there is little information regarding the immune response to repeated immunization with CAIV-T. OBJECTIVE: To determine the antibody response to repeated immunization with CAIV-T and to compare this with the response after the first CAIV-T immunization. DESIGN AND METHODS: Healthy children were offered CAIV-T immunization for 4 consecutive years, and blood samples were taken from a subset in Years 1, 2 and 4. In Year 4, 156 similarly aged children who had not received influenza vaccine previously were immunized with the same CAIV-T. RESULTS: The H3N2 and B components of the CAIV-T induced high antibody titers in Year 1 that were maintained during 4 years. The H1N1 titers were lower than the H3N2 or B titers. Comparison of the group immunized for 4 consecutive years with the group immunized for the first time revealed the following: (1) before immunization yearly immunized subjects were more likely to be seropositive to each of the three vaccine strains than those immunized for the first time (P < 0.05 for each); (2) after immunization the percentage of seropositive subjects to each of the strains was similar; (3) after immunization titers were higher in the subjects immunized for the first time than those immunized yearly (P < 0.05 for H3N2 and B). CONCLUSION: Yearly vaccination with CAIV-T induced high antibody titers, especially to the H3N2 and B strains in the vaccines. The titers in those immunized with CAIV-T for the first time were higher than in those immunized for 4 consecutive years.

Administration, Intranasal↗

PubMed2003

Induction of protective immunity against malaria by priming-boosting immunization with recombinant cold-adapted influenza and modified vaccinia Ankara viruses expressing a CD8+-T-cell epitope derived from the circumsporozoite protein of Plasmodium yoelii.

We immunized mice with an attenuated (cold-adapted) influenza virus followed by an attenuated vaccinia virus (modified vaccinia virus Ankara), both expressing a CD8(+)-T-cell epitope derived from malaria sporozoites. This vaccination regimen elicited high levels of protection against malaria. This is the first time that the vaccine efficacy of a recombinant cold-adapted influenza virus vector expressing a foreign antigen has been evaluated.

Adaptation, Physiological↗

PubMed1990

[Features of mutated changes of genomic RNA of cold-adapted and hr-variants of influenza group A virus, detected by RNA:RNA hybridization].

The presence of mutations in the majority of the genes of cold-adapted strains A/Leningrad/134/17/57 (H2N2), A/Leningrad/134/47/57 (H2N2) and A/PR/8/59/1 (H1N1) of influenza A virus has been demonstrated by the RNA-RNA hybridization with the subsequent electrophoresis of double-stranded RNA in 7.5% polyacrylamide gel. The strains were cultivated 17, 47 and 59 passages in the chicken embryos at 25 degrees C. In the genomes of variants passaged in chicken embryos at optimal temperature of incubation 36 degrees C (hr-variants) the used technique permits identification of a single mutant gene. The obtained data suppose the attenuation of cold-adapted vaccine strains of influenza A virus and their high genetic stability to be a result of selection of the variants obtaining multiple mutations in the genome during passaging of the virions at cold temperature. The attenuation of hr-variants is defined by 1-2 mutations (first of all in HA-gene) that makes understandable their inability to serve as donors for recombinant live influenza vaccines construction.

Antigens, Viral↗

PubMed1982

Infant rat model of attenuation for recombinant influenza viruses prepared from cold-adapted attenuated A/Ann Arbor/6/60.

The pathogenicity of 6 wild-type influenza A viruses and 21 recombinant strains prepared from wild-type viruses and cold-adapted A/Ann Arbor/6/60 virus for infant rats was determined. Thus, the titers of virus present in the turbinates and lungs of virus-infected animals was measured serially for 5 days after intranasal infection, and the ability of virus strains to promote subsequent systemic bacterial infection by Haemophilus influenzae was measured at 48 h after virus infection. The results obtained were assessed with reference to the genetic constitution of the virus strains and to virus virulence for volunteers. The results showed that virulent viruses grew to relatively high titers in rat turbinates and significantly promoted systemic infection by H. influenzae. In contrast, attenuated strains grew to lower titers and failed to promote systemic H. influenzae infection. For the strains tested, the results showed clear differences for attenuated and virulent strains, and the model was a reliable indication of virulence for humans. Although the virulent strains tended to grow to higher titers in rat lungs than did attenuated strains, exceptions were found, and this measurement could not reliably discriminate virulent and attenuated virus strains. The results suggest that infant rats can be used to assess the virulence of cold-adapted recombinant influenza virus strains, and thus, they can facilitate the development of such strains for vaccine production.

Animals↗

PubMed2002

Universal vaccination of healthy children against influenza: a role for the cold-adapted intranasal influenza vaccine.

The incidence of influenza in children well exceeds that of the elderly and has been identified as the basis for 20% of doctor visits for children during the winter. The disease results in over 100 hospitalizations per 100000 person-months in children <2 years of age. Furthermore, children serve as the major vector in the community; thus, influenza in children results in significant costs to society. Although efficacious, the current intramuscular, inactivated influenza vaccine is infrequently used in children, and is currently targeted only at children at high risk and those who are household members of such individuals. Experts believe that vaccinating only high risk individuals has little impact on the cycle of annual epidemics, but that universal vaccination of children may very well have a substantial impact. Experimental data support this. A recently published cost-benefit analysis indicated that routine, school-aged vaccination through individual visits to a clinician would save 4 US dollars per child vaccinated. A group program such as a school-based one would save 35 US dollars. One obstacle to universal vaccination includes the real and perceived resistance to the addition of yet another annual injection to the already crowded schedule of routine childhood immunizations. Nearing licensure is an intranasal, live attenuated, cold-adapted intranasal influenza vaccine. Cold-adaptation prevents replication in the lower respiratory tract. Trials have demonstrated immunogenicity, safety, and tolerability in adults as well as children. Placebo-controlled trials have shown efficacy rates of 83 to 94%. This novel vaccine addresses obstacles to universal childhood immunization and would permit a program of routine use that would dramatically reduce transmission and stem epidemics of influenza.

Administration, Intranasal↗

PubMedDate not supplied

[Development of a live culture of cold-adapted reassortant influenza vaccines].

Optimal conditions for the cultivation of the MDCK cell lines in the laboratory spinner or by using the Eagle-MEM with or without fetal serum were worked out. The cold-adapted reassortant vaccine strains of virus influenza A/H1N1, A/H3N2 and B are well replicated in the MDCK cells both in a monolayer and in the spinner by using the serum-free medium. A maximum virus titer depends on a multiplicity of infection used in a fetal medium and on the addition of trypsin. Under the optimal conditions, the titer of the studied cold-adapted reassortants, while using a serum-free medium, reaches as much as 10(9.0)-10(9.5) EID50/ml.

Adaptation, Physiological↗

PubMed2005

Total lactate dehydrogenase activity of tail muscle is not cold-adapted in nocturnal lizards from cool-temperate habitats.

The dependence of metabolic processes on temperature constrains the behavior, physiology and ecology of many ectothermic animals. The evolution of nocturnality in lizards, especially in temperate regions, requires adaptations for activity at low temperatures when optimal body temperatures are unlikely to be obtained. We examined whether nocturnal lizards have cold-adapted lactate dehydrogenase (LDH). LDH was chosen as a representative metabolic enzyme. We measured LDH activity of tail muscle in six lizard species (n=123: three nocturnal, two diurnal and one crepuscular) between 5 and 35 degrees C and found no differences in LDH-specific activity or thermal sensitivity among the species. Similarly, the specific activity and thermal sensitivity of LDH were similar between skinks and geckos. Similar enzyme activities among nocturnal and diurnal lizards indicate that there is no selection of temperature specific LDH enzyme activity at any temperature. As many nocturnal lizards actively thermoregulate during the day, LDH may be adapted for a broad range of temperatures rather than adapted specifically for the low temperatures encountered when the animals are active. The total activity of LDH in tropical and temperate lizards is not cold-adapted. More data are required on biochemical adaptations and whole animal thermal preferences before trends can be established.

Adaptation, Physiological↗

PubMed2005

Pulmonary CD4+ cytokine responses in mice reveal differences in the relative immunogenicity of cold-adapted influenza A vaccine donor strains.

We previously described differences in the 50% protective dose and isotype-specific antibody secreting cell (ASC) responses to US and Russian influenza A cold-adapted (ca) donor strains in the lungs of BALB/c mice [Wareing MD, Watson JM, Brooks MJ, Tannock GA. Immunogenic and isotype-specific responses to Russian and US cold-adapted influenza A vaccine donor strains A/Leningrad/134/17/57, A/Leningrad/134/47/57, and A/Ann Arbor/6/60 (H2N2) in mice. J Med Virol 2001;65(1):171-7]. A/Leningrad/134/17/57(Len/17-ca) was shown to be a superior immunogen to A/Leningrad/134/47/57-ca (Len/47-ca), which, in turn, was superior to A/Ann Arbor/6/60-ca (AA-ca) but no other comparative data exist. In order to extend our findings and determine a means for selecting the most immunogenic ca influenza A vaccine, the intracellular cytokine responses by CD4+ and CD8+ T cells to AA-ca, Len/47-ca and Len/17-ca and their respective wild-type parental viruses were compared in mice. Day 5 after infection with Len/17-ca, when levels of IL-2, -4 and -10 were highest in the mediastinal lymph nodes (MLN) and lungs, was chosen as the optimum time to harvest lymphocytes and 72 h was determined to be the optimum re-stimulation period for lymphocytes by APCs. Under these conditions, the frequency of CD4+ and CD8+ cells expressing cytokines was highest in the lungs compared with the MLN. A dominant IL-6 response was induced, although all virus strains induced a Th1/Th2 cytokine profile. While the CD8+ cytokine response appeared non-specific, the cytokine response elicited in the lungs by CD4+ cells to Len/17-ca-inoculation was greater than that induced by Len/47-ca, or AA/ca. The CD4+ cytokine response in the lungs may be a useful measure of immunogenicity to determine the most effective influenza reassortant for inclusion in vaccines.

Animals↗

PubMed1985

Comparative studies of A/Leningrad/134/57 wild-type and 47-times passaged cold-adapted mutant influenza viruses: oligonucleotide mapping and RNA-RNA hybridization studies.

Direct biochemical evidence for the existence of mutations in five of the RNA segments of the A/Leningrad/134/57 cold-adapted 47th passage mutant as compared with its wild-type progenitor has been obtained using two techniques. T1 oligonucleotide mapping of total viral RNA as well as of individual RNA segments revealed changes in RNAs 4, 5 and 6. Analysis of S1 nuclease-treated RNA-RNA hybrids on polyacrylamide gels revealed changes in at least one of the polymerase genes as well as in RNAs 4, 5, 6 and 7. These findings provide a direct demonstration for the existence of multiple mutations in the cold-adapted mutant vaccine strain.

Cold Temperature↗