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1.
Rev. ing. bioméd ; 9(18): 73-80, jul.-dic. 2015. graf
Article in Spanish | LILACS | ID: lil-769181

ABSTRACT

En este trabajo se presentan los resultados obtenidos tras analizar la información recolectada en once instituciones prestadoras de servicios de salud (IPS) en la ciudad de Cali y municipios aledaños, sobre tres elementos clave para la buena práctica de la Ingeniería Clínica: adquisición de tecnología, gestión de mantenimiento y formación del personal. Se realizó una comparación entre las prácticas actuales de IC en las IPS encuestadas y las prácticas propuestas en la literatura existente. Se propone además una serie de aspectos a tomar en cuenta con miras a mejorar el desempeño de los departamentos de IC tanto en la ciudad como en el país.


This paper summarizes the results obtained after analyzing the information gathered in eleven institutions providing health services (IPS, in Colombia) in the city of Cali and surrounding municipalities, three key elements for good clinical engineering practice are presented: Acquisition technology, management, maintenance and staff training. A comparison between current practices in the surveyed IC at IPS and practices proposed in the literature was conducted. It also proposes a number of aspects to consider in order to improve performance of both IC departments in the city and in the country.


Este artigo apresenta os resultados obtidos depois de analisar as informações coletadas em onze instituições prestadoras de serviços de saúde (IPS), na cidade de Cali e municípios vizinhos, sobre três elementos-chave para a boa prática de engenharia clínica: aquisição de tecnologia, gestão de manutenção e treinamento de pessoal. Uma comparação foi feita entre as práticas atuais nas IPS e práticas propostos na literatura atual. Ele também propõe uma série de aspectos a considerar, a fim de melhorar o desempenho dos departamentos IC tanto na cidade quanto no país.

2.
Int J Obes Suppl ; 5(Suppl 2): S107-14, 2015 Dec.
Article in English | MEDLINE | ID: mdl-27152178

ABSTRACT

OBJECTIVES: Within the global context of the nutrition and physical activity transition it is important to determine the relationship between adiposity and active school transport (AST) across different environmental and socio-cultural settings. The present study assessed the association between adiposity (that is, body mass index z-score (BMIz), obesity, percentage body fat (PBF), waist circumference) and AST in 12 country sites, in the International Study of Childhood Obesity, Lifestyle and the Environment (ISCOLE). METHODS: The analytical sample included 6797 children aged 9-11 years. Adiposity indicators included, BMIz calculated using reference data from the World Health Organization, obesity (BMIz ⩾+2 s.d.), PBF measured using bioelectrical impedance and waist circumference. School travel mode was assessed by questionnaire and categorized as active travel versus motorized travel. Multilevel linear and non-linear models were used to estimate the magnitude of the associations between adiposity indicators and AST by country site and sex. RESULTS: After adjusting for age, sex, parental education and motorized vehicle availability, children who reported AST were less likely to be obese (odds ratio=0.72, 95% confidence interval (0.60-0.87), P<0.001) and had a lower BMIz (-0.09, s.e.m.=0.04, P=0.013), PBF (least square means (LSM) 20.57 versus 21.23% difference -0.66, s.e.m.=0.22, P=0.002) and waist circumference (LSM 63.73 cm versus 64.63 cm difference -0.90, s.e.m.=0.26, P=0.001) compared with those who reported motorized travel. Overall, associations between obesity and AST did not differ by country (P=0.279) or by sex (P=0.571). CONCLUSIONS: AST was associated with lower measures of adiposity in this multinational sample of children. Such findings could inform global efforts to prevent obesity among school-age children.

3.
J Hazard Mater ; 186(2-3): 1652-9, 2011 Feb 28.
Article in English | MEDLINE | ID: mdl-21216096

ABSTRACT

The aim of this work was to evaluate the efficiency of three chemical oxidation processes for increasing the biodegradability of aqueous diethanolamine solutions (aqueous DEA solutions), to be used as pre-treatments before a biological process. The raw aqueous DEA solution, sourced from a sour gas sweetening plant at a Mexican oil refinery, was first characterized by standardized physico-chemical methods. Then experiments were conducted on diluted aqueous DEA solutions to test the effects of Fenton's reagent, ozone and ozone-hydrogen peroxide on the removal of some physicochemical parameters of these solutions. Lastly, biodegradability tests based on Dissolved Organic Carbon Die Away OECD301-A, were carried out on a dilution of the raw aqueous DEA solution and on the treated aqueous DEA solutions, produced by applying the best experimental conditions determined during the aforementioned oxidation tests. Experimental results showed that for aqueous DEA solutions treated with Fenton's reagent, the best degradation rate (70%) was obtained at pH 2.8, with Fe(2+) and H(2)O(2) at doses of 1000 and 10,000 mg/L respectively. In the ozone process, the best degradation (60%) was observed in aqueous DEA solution (100 mg COD/L), using 100 mg O(3)/L at pH 5. In the ozone-hydrogen peroxide process, no COD or DOC removals were observed. The diluted spent diethanolamine solution showed its greatest increase in biodegradability after a reaction period of 28 days when treated with Fenton's reagent, but after only 15 days in the case of ozonation.


Subject(s)
Biodegradation, Environmental/drug effects , Ethanolamines/chemistry , Hydrogen Peroxide/chemistry , Iron/chemistry , Ozone/chemistry , Petroleum/analysis , Industry , Mexico , Models, Statistical , Oxidation-Reduction , Oxygen/analysis , Oxygen/chemistry , Solutions
4.
Article in English | MEDLINE | ID: mdl-17270501

ABSTRACT

The venom from the Brazilian scorpion Tityus stigmurus was fractionated by high performance liquid chromatography (HPLC) and the corresponding components were used for molecular mass determination using electrospray ion trap mass spectrometry. One hundred distinct components were clearly assigned showing molecular masses from 216.5 to 44,800.0 Da. Fifteen new components were isolated and sequenced, four of them to completion: Tst-3 (similar to Na(+) channel specific scorpion toxins), Tst-17 (a K(+) channel blocking peptide similar to Tc1), Tst beta KTx (a peptide with identical sequence as that of TsTX-K beta toxin earlier described to exist in T. serrulatus venom) and finally a novel proline-rich peptide of unknown function. Among the eleven components partially sequenced were two enzymes: hyaluronidase and lysozyme. The first enzyme has a molecular mass of 44,800.0 Da. This enzyme showed high activity against the substrate hyaluronan in vitro. Amino acid sequence of the second enzyme showed that it is similar to other known lysozymes, with similar molecular mass and sequence to that of bona fide lysozymes reported in public protein data banks. Finally, this communication reports a correlation among HPLC retention times and molecular masses of folded scorpion toxins as well as a comparative structural and physiological analysis of components from the venom of several species of the genus Tityus.


Subject(s)
Insect Proteins/chemistry , Potassium Channel Blockers/chemistry , Proteomics , Scorpion Venoms/chemistry , Scorpions , Amino Acid Sequence , Animals , Cells, Cultured , Chromatography, High Pressure Liquid , Electrophysiology , Hyaluronoglucosaminidase/analysis , Insect Proteins/pharmacology , Molecular Sequence Data , Molecular Weight , Muramidase/analysis , Patch-Clamp Techniques , Peptide Mapping , Potassium Channel Blockers/pharmacology , Scorpion Venoms/pharmacology , Shaker Superfamily of Potassium Channels/drug effects , Shaker Superfamily of Potassium Channels/metabolism , Species Specificity , Spectrometry, Mass, Electrospray Ionization , Spodoptera/cytology , Spodoptera/drug effects
5.
Rev Gastroenterol Mex ; 70(4): 387-92, 2005.
Article in Spanish | MEDLINE | ID: mdl-17058976

ABSTRACT

UNLABELLED: Colonic transit time (CTT) is determined by multiple factors; currently, normal values for the Mexican population are not available. In order to get an estimate one must look at the values reported in the international literature, but cultural, ethnical, nutritional and economic differences may lead to different values. OBJECTIVE: To determine the normal values of colonic transit time in healthy people in Mexico City by the use of radiopaque markers. PATIENTS AND METHODS: Prospective, longitudinal and observational study, which included healthy patients ranging from 18 to 60 years old; excluding pregnant women. The whole group of patients was given before breakfast a gelatin capsule which had 20 radiopaque markers inside -the markers were each 2mm long, and were made by the researcher-. After that, they were taken a simple abdominal X-ray film every 24 hours until they totally eliminated the markers. Their eating and defecation habits were evaluated and also the total amount of liquid they consumed. Inferential statistics were used; data was validated with both parametric and non-parametric tests, considering a significance of p < 0.05. RESULTS: A hundred patients were included in the sample in which 48% were female and 52% male, they were divided in three groups: group A (31%)from 18 to 25 years, group B (37%)from 26 to 40 and group C (32%)from 41 to 60 years; there were no important differences in their water consumption, which was in average of 1.87 lts. in 24 hours; also, there were no considerable differences regarding to their meat, vegetables and fruits' consumption, which was in average of 4.4 times a week; the whole group eliminated the markers according to X-rays which was in 54% after 72 hrs, 45% after 48 hrs and 1% after 24 hrs. We can observe an increase of the CTT related to age: in group C 94% eliminated the markers after 72 hrs and there was no significant difference (statistically) with regards to the other groups. A tendency of an increase of CTT with regards to age was observed: in group A, 80% eliminated the markers after 48 hrs, in group B 49% eliminated them after 48 hrs and 51% after 72 hrs and, in group C, 94% eliminated them after 72 hrs without any statistically significant differences among the study groups. CONCLUSION: The CTT in healthy patients is in a 100% of the cases studied lower or equal to 72 hrs with a tendency to increase in relation to age.


Subject(s)
Colon/physiology , Gastrointestinal Transit , Adolescent , Adult , Female , Humans , Male , Mexico , Middle Aged , Prospective Studies , Reference Values , Urban Population
6.
Virus Res ; 76(1): 103-13, 2001 Jul.
Article in English | MEDLINE | ID: mdl-11376850

ABSTRACT

To study the process of feline immunodeficiency virus (FIV) assembly, we examined the suitability of the vaccinia vector system to reproduce FIV particle formation. To this end, we constructed a recombinant vaccinia virus carrying the FIV gag gene. Biochemical and electron microscopy analyses of cells infected with this recombinant virus showed that the FIV Gag polyprotein self-assembled into lentivirus-like particles that were released into the culture medium. As a first step in the identification of molecular determinants in FIV Gag that are involved in virus assembly, we performed a site-directed mutagenesis analysis of the N-terminal matrix (MA) domain of the FIV Gag precursor. To this end, a series of amino acid substitutions and small in-frame deletions were introduced into the FIV MA and the mutated FIV gag gene constructs were expressed by means of the vaccinia system. Characterization of the assembly phenotype of these FIV Gag mutants led to the identification of amino acidic regions within the MA domain that are necessary for efficient transport of the Gag precursor to the plasma membrane and particle assembly. Our results reveal the role that the FIV MA plays in virus morphogenesis and contribute to the understanding of the assembly process in non-primate lentiviruses.


Subject(s)
Gene Products, gag/metabolism , Immunodeficiency Virus, Feline/metabolism , Immunodeficiency Virus, Feline/ultrastructure , Mutation/genetics , Viral Matrix Proteins/metabolism , Virus Assembly , Amino Acid Sequence , Animals , Cell Line , DNA, Recombinant/genetics , Fibroblasts , Gene Products, gag/chemistry , Gene Products, gag/genetics , Genes, gag/genetics , Genetic Vectors/genetics , Immunodeficiency Virus, Feline/genetics , Microscopy, Electron , Molecular Sequence Data , Protein Structure, Tertiary , Thymidine Kinase/genetics , Transfection , Vaccinia virus/genetics , Viral Matrix Proteins/chemistry , Viral Matrix Proteins/genetics
7.
Virology ; 283(2): 253-61, 2001 May 10.
Article in English | MEDLINE | ID: mdl-11336550

ABSTRACT

The mechanism by which lentivirus envelope (Env) glycoproteins are packaged into budding virions is poorly understood. Simian immunodeficiency virus (SIV) contains an Env protein with an unusually long cytoplasmic tail. To investigate the role of this domain in the incorporation of the SIV Env into virions, we generated a series of SIV Env mutants carrying small in-frame deletions within the cytoplasmic domain. The effects of these mutations on Env synthesis, processing, and association with Gag particles were analyzed by means of the vaccinia virus expression system. All of the mutant Env glycoproteins were synthesized and processed in a manner similar to that of the wild-type Env. However, deletions affecting domains C-terminal to residue 832 in the SIV Env protein significantly impaired Env incorporation into particles. Cell surface biotinylation assays showed that this phenotype could not be attributed to inefficient cell surface expression of the Env mutants. Furthermore, when the Env deletion mutants were tested for their ability to mediate virus entry in single-cycle infectivity assays, those mutations that impaired Env incorporation also caused a severe defect in virus infectivity. Our results suggest that domains in the C-terminal third of the SIV Env protein are required for Env incorporation into particles and Env-mediated virus entry.


Subject(s)
Membrane Glycoproteins/chemistry , Membrane Glycoproteins/metabolism , Retroviridae Proteins/chemistry , Retroviridae Proteins/metabolism , Simian Acquired Immunodeficiency Syndrome/virology , Simian Immunodeficiency Virus/pathogenicity , Virion/metabolism , Animals , Cells, Cultured , Chlorocebus aethiops , Cytoplasm/chemistry , Membrane Glycoproteins/genetics , Protein Structure, Tertiary , Rats , Retroviridae Proteins/genetics , Sequence Deletion , Simian Immunodeficiency Virus/genetics , Simian Immunodeficiency Virus/metabolism , Vaccinia virus/genetics
8.
AIDS Res Hum Retroviruses ; 17(17): 1615-24, 2001 Nov 20.
Article in English | MEDLINE | ID: mdl-11779349

ABSTRACT

Simian immunodeficiency viruses (SIVs) have an envelope (Env) glycoprotein with an unusually long cytoplasmic domain of 164 amino acids. In this article, we have characterized a series of SIV Env truncation mutants in which the cytoplasmic domain was progressively shortened from its carboxyl terminus by 20 amino acids. Expression by means of the vaccinia virus system showed that all of the SIV Env mutants were expressed and processed into the surface and transmembrane (TM) subunits. When the ability of the Env mutants to associate with SIV Gag particles was examined, we found that deletion of 20 to 80 residues from the carboxyl terminus of the SIV TM cytoplasmic tail abrogated the incorporation of the Env glycoprotein into particles. By contrast, further truncation of the SIV TM protein by 100 to 140 amino acids restored the ability of the Env protein to associate with Gag particles. Interestingly, mutants bearing a 44- or 24-amino acid cytoplasmic domain were incorporated at levels significantly higher than those of the wild-type Env. Single-cycle infectivity assays showed that Env mutants bearing cytoplasmic tails of 144 to 64 amino acids were highly inefficient at mediating virus entry. By contrast, truncation of the cytoplasmic domain to 44 or 24 amino acids drastically enhanced virus infectivity with respect to that conferred by the full-length Env protein. Our results demonstrate that small variations in the length of the SIV Env cytoplasmic domain dramatically influence Env-mediated viral functions.


Subject(s)
Mutation , Simian Immunodeficiency Virus/pathogenicity , Viral Envelope Proteins/chemistry , Viral Envelope Proteins/genetics , Animals , Cell Line , Cell Membrane/metabolism , Gene Products, gag/metabolism , Humans , Simian Acquired Immunodeficiency Syndrome/virology , Simian Immunodeficiency Virus/chemistry , Simian Immunodeficiency Virus/genetics , Viral Envelope Proteins/metabolism , Virion/metabolism
9.
Ginecol Obstet Mex ; 66: 221-6, 1998 Jun.
Article in Spanish | MEDLINE | ID: mdl-9679396

ABSTRACT

Diabetes mellitus during pregnancy could result in severe or fatal complications to mother or the unborn product, like polyhydramnios, preeclampsia, abortion, neonatal asphyxia, macrosomia, stillbirth, and others, therefore is very important the early detection and treatment of diabetes. Gestacional Diabetes Mellitus (GDM) is the carbohydrate intolerance of variable severity first recognized during pregnancy. The screening test consist of 50 g of oral glucose and a plasma glucose measurement at one hour, regardless of the time of the last meal, and this may do in all pregnancies between 24 and 28 weeks of gestation. If plasma glucose level above 140 mg/dl results, a oral glucose tolerance test with 100 g must be done. This is the GDM diagnostic test. The risk factors for gestacional diabetes (older than 30 years of age, obesity, arterial hypertension, glucosury, previous GDM, family history of diabetes, family history of macrosomia) identify only 50% of pregnancies with gestacional diabetes, therefore, is necessary to screen all pregnancies who become pregnant, a strict control before pregnant is indispensable, with aim to slow congenital malformations probability and another complications. Gestacional diabetes prevalence in hispanic women in the U.S.A. is 12.3 percent. Diabetes mellitus prevalence in Mexico is about 2-6 percent. The goal of management of diabetes during pregnancy is the maintainance of fasting plasma glucose 105 mg/dl and 120 mg/dl two hours after meals. Treatment consist in diabetes education, diet with caloric needs calculation, exercise, and occasionally insulin. Is necessary the prenatal monitoring, the supervision of delivery or cesarean metabolic changes, and the postnatal monitoring of the mother and product.


Subject(s)
Pregnancy in Diabetics/blood , Adult , Age Factors , Diabetes Complications , Female , Fetal Macrosomia/etiology , Follow-Up Studies , Glucose Tolerance Test , Humans , Infant, Newborn , Insulin/blood , Obesity , Pregnancy , Risk Factors
10.
Virology ; 240(1): 27-35, 1998 Jan 05.
Article in English | MEDLINE | ID: mdl-9448686

ABSTRACT

In the late stages of replication of the simian immunodeficiency viruses (SIV), the matrix protein (MA) plays a central role in the transport of Pr55gag to the plasma membrane, assembly of virus particles, and incorporation of the envelope glycoprotein into particles. Targeting of Pr55gag to the plasma membrane is mediated by two motifs within the MA protein: the N-terminal myristate and a cluster of positively charged amino acids. In this report, we characterized the assembly phenotype of an SIV Gag mutant (L8Q) carrying the single amino acid substitution of glutamine for leucine at position 8 in the MA domain. The hydropathic profile of the mutated MA protein indicated that the L8Q amino acid change disrupts the hydrophobic character of the region comprising the first 10 residues of the protein. Expression of mutant L8Q Gag protein in CV-1 cells, by means of the vaccinia virus vector system, resulted in efficient synthesis and N-myristylation of Pr55gag. However, this mutation severely impaired particle production, as inferred from both biochemical and electron microscopy analyses. Cellular fractionation assays revealed that in cells expressing mutant L8Q, the proportion of cytosol-associated Pr55gag was significantly increased compared to that observed upon expression of wild-type Gag. Furthermore, mutant L8Q Gag partitioned onto cytosol and membrane fractions in a manner similar to nonmyristylated Gag polyprotein. Taken together, these results indicate that the L8Q mutation reduces the membrane-binding capacity of the Gag precursor. It is therefore likely that in the SIV MA, in addition to the N-myristate group, the hydrophobicity of the neighboring region is important for efficient association of Pr55gag with the plasma membrane.


Subject(s)
Gene Products, gag/metabolism , Leucine , Myristic Acid/metabolism , Protein Processing, Post-Translational , Simian Immunodeficiency Virus/physiology , Viral Matrix Proteins/metabolism , Virus Replication , Amino Acid Sequence , Amino Acid Substitution , Animals , Cell Line , Chlorocebus aethiops , Kidney , Molecular Sequence Data , Mutagenesis, Site-Directed , Protein Conformation , Rats , Recombinant Proteins/chemistry , Recombinant Proteins/metabolism , Simian Immunodeficiency Virus/ultrastructure , Transfection , Vaccinia virus , Viral Matrix Proteins/chemistry
11.
J Gen Virol ; 78 ( Pt 8): 1949-55, 1997 Aug.
Article in English | MEDLINE | ID: mdl-9266993

ABSTRACT

VP6, the major capsid protein of rotavirus, oligomerizes into trimers that constitute the intermediate shell of the virions. In order to map functional domains in this protein, we introduced seven internal in-frame deletions within the coding region of gene 6 of human rotavirus strain Wa. Regions of homology among the VP6 proteins of group A and group C rotaviruses were targeted for deletion mutagenesis. The mutant VP6 proteins were expressed in mammalian cells using the recombinant vaccinia virus system and were examined for their ability to oligomerize into trimers as well as to assemble into double-layered virus-like particles upon coexpression with the rotavirus core protein VP2. Deletions that abolished trimerization defined a domain (residues 246 to 314) that maps within a larger region previously found to be critical for oligomerization (amino acids 105 to 328). When the capacity of each mutant to assemble into double-layered virus-like particles was analysed, three different assembly phenotypes were observed. Phenotype I was represented by two deletion mutants lacking residues 246 to 250 and 308 to 314 that produced particles with efficiencies similar to that of wild-type VP6. Phenotype II, characterized by a moderate decrease in the efficiency of particle assembly with respect to that of wild-type VP6, included two mutants with deletions at the C terminus of the protein. Phenotype III was exhibited by three mutants whose abilities to assemble into double-layered virus-like particles were drastically impaired. Two of these mutants define a previously unidentified assembly domain (amino acids 122 to 147) at the N terminus of rotavirus VP6.


Subject(s)
Antigens, Viral , Capsid Proteins , Capsid/chemistry , Capsid/metabolism , Rotavirus/metabolism , Amino Acid Sequence , Animals , Capsid/biosynthesis , Cell Line , Chlorocebus aethiops , Genetic Vectors , Humans , Macromolecular Substances , Mammals , Molecular Sequence Data , Mutagenesis, Site-Directed , Recombinant Proteins/biosynthesis , Recombinant Proteins/chemistry , Recombinant Proteins/metabolism , Rotavirus/genetics , Sequence Deletion , Transfection , Vaccinia virus
12.
J Virol ; 70(9): 6384-9, 1996 Sep.
Article in English | MEDLINE | ID: mdl-8709267

ABSTRACT

The matrix domain (MA) of the simian immunodeficiency virus (SIV) is encoded by the amino-terminal region of the Gag polyprotein precursor and is the component of the viral capsid that lines the inner surface of the virus envelope. To define domains of the SIV MA protein that are involved in virus morphogenesis, deletion and substitution mutations were introduced in this protein in the context of a gag-protease construct and expressed in the vaccinia virus vector system. The MA mutants were characterized with respect to synthesis and processing of the Gag precursor, assembly and release of virus-like particles, and incorporation of the envelope (Env) glycoprotein into particles. We have identified two regions of the SIV MA which are critical for particle formation. Both domains are located in a central hydrophobic alpha-helix of the SIV MA, according to data on the structure of this protein. In addition, we have characterized a domain whose mutation impairs the incorporation of SIV Env glycoproteins with long transmembrane cytoplasmic tails into particles. Interestingly, these mutant particles retained the ability to associate with SIV Env proteins with short cytoplasmic tails.


Subject(s)
Gene Products, env/biosynthesis , Gene Products, gag/biosynthesis , Simian Immunodeficiency Virus/metabolism , Viral Matrix Proteins/metabolism , Amino Acid Sequence , Animals , Capsid/biosynthesis , Cell Line , Chlorocebus aethiops , Gene Products, gag/genetics , Genes, gag , HIV-1/metabolism , Humans , Molecular Sequence Data , Mutagenesis, Site-Directed , Protein Precursors/metabolism , Recombinant Proteins/chemistry , Recombinant Proteins/metabolism , Sequence Homology, Amino Acid , Viral Matrix Proteins/chemistry
13.
J Gen Virol ; 76 ( Pt 9): 2357-60, 1995 Sep.
Article in English | MEDLINE | ID: mdl-7561777

ABSTRACT

Development in mammalian cells of a recombinant expression system that mimics the rotavirus capsid assembly process would be advantageous for studying the structural requirements for particle formation. To this end, we investigated the ability of a recombinant vaccinia virus system to produce double-layered virus-like particles. The genes coding for VP2 and VP6 proteins of the human rotavirus strain Wa were cloned and used to generate recombinant vaccinia viruses. Metabolic labelling of CV-1 cells infected with these recombinant viruses followed by immunoprecipitation with a polyclonal antiserum directed to Wa virus showed that VP2 and VP6 were efficiently expressed. The recombinant proteins were similar in size and immunoreactivity to authentic rotavirus proteins. Biochemical and electron microscopy analyses demonstrated that simultaneous expression of VP2 and VP6 in mammalian cells resulted in the formation of intracellular spherical particles resembling double-layered rotavirus particles.


Subject(s)
Antigens, Viral , Capsid/biosynthesis , Rotavirus/physiology , Animals , Base Sequence , Capsid/genetics , Capsid Proteins , Cell Line , DNA Primers , DNA, Viral , Humans , Mammals , Molecular Sequence Data , Recombinant Fusion Proteins/genetics , Rotavirus/genetics , Rotavirus/ultrastructure , Vaccinia virus/genetics , Virion/ultrastructure , Virus Replication
14.
Virology ; 210(2): 501-7, 1995 Jul 10.
Article in English | MEDLINE | ID: mdl-7618287

ABSTRACT

The matrix protein (MA) of human and simian immunodeficiency viruses (HIV and SIV) is encoded by the amino-terminal region of the Gag precursor and has been suggested to be involved in different processes during the early and late stages of the virus life cycle. The MA protein of SIV contains three cysteine residues at positions 57, 83, and 87, which are also highly conserved among HIV-2 isolates. In order to study the functional significance of these residues in virus morphogenesis, a series of mutations affecting the cysteines of SIV MA were introduced into a gag-protease construct and expressed in the vaccinia vector system. The MA mutants were assayed for their ability to synthesize and process the Gag polyprotein precursor as well as to release particles into the culture medium. In addition, the incorporation of the envelope glycoprotein (Env) into the Gag-made particles was investigated. Substitution of alanine for cysteine 87 had little effect on particle release and Env glycoprotein association. By contrast, the individual replacement of cysteines 57 or 83 by alanine, as well as the simultaneous mutation of cysteines 83 and 87, significantly reduced the ability of Gag polypeptides to produce extracellular particles. Assembly into particles appeared to be also affected, albeit to a lesser extent, when both cysteines 57 and 83 were replaced by alanine. Furthermore, substitution of cysteine 83 in the SIV MA domain was found to be detrimental to Gag polyprotein processing. Analysis of the Env glycoprotein association with recombinant particles revealed that this process was moderately affected in the case of the double mutants lacking cysteines 57 and 83, or cysteines 57 and 87, and the cysteine-minus triple mutant. Our results suggest that the conserved cysteines 57 and 83 in the MA domain are important for efficient SIV Gag particle production.


Subject(s)
Conserved Sequence/genetics , Cysteine/physiology , DNA Mutational Analysis , Membrane Glycoproteins , Simian Immunodeficiency Virus/physiology , Viral Envelope Proteins , Viral Matrix Proteins/genetics , Virus Replication/genetics , Amino Acid Sequence , Base Sequence , Cell Line , Gene Products, env/metabolism , Gene Products, gag/biosynthesis , Gene Products, gag/metabolism , Genes, gag/genetics , Genetic Vectors/genetics , HIV Envelope Protein gp120/analysis , Molecular Sequence Data , Morphogenesis , Mutation/physiology , Protein Processing, Post-Translational , Simian Immunodeficiency Virus/genetics , Vaccinia virus/genetics , Viral Matrix Proteins/physiology , Virion
15.
J Gen Virol ; 76 ( Pt 1): 221-4, 1995 Jan.
Article in English | MEDLINE | ID: mdl-7844537

ABSTRACT

A porcine rotavirus strain, CN86, originally isolated from rotavirus-infected piglets in Argentina, has been shown to possess unique characteristics. It was the first animal strain described to be antigenically related to human serotype G1 and the standard counterpart of another porcine strain showing rearrangement of genome segment 11. Owing to these features, molecular characterization of this virus seemed relevant. The gene encoding the major inner capsid protein, VP6, was cloned and its nucleotide sequence was determined. Comparative analysis of the deduced amino acid sequence of CN86 VP6 with those representing the four different subgroups showed that it is more closely related to subgroup II human Wa and porcine Gottfried strains, albeit to a lesser extent than they are to each other. Despite exhibiting sequence divergence, CN86 VP6 has 12 out of the 14 residues expected to be conserved in strains bearing subgroup II specificity. Interestingly, CN86 VP6 shows a high degree of homology with VP6 of porcine strain YM rotavirus which, although being closely related to subgroup II strains, has been serologically characterized as subgroup I. Subgroup II reactivity of CN86 strain, predicted by sequence analysis, was confirmed by ELISA with subgroup-specific monoclonal antibodies. Taken together, our results provide evidence for the existence of a human-pig lineage for rotavirus gene 6.


Subject(s)
Antigens, Viral , Capsid Proteins , Capsid/chemistry , Rotavirus/chemistry , Swine/virology , Amino Acid Sequence , Animals , Capsid/genetics , Conserved Sequence , Molecular Sequence Data , Rotavirus/genetics , Sensitivity and Specificity
16.
Rev. chil. anest ; 20(1): 21-5, jun. 1991. tab
Article in Spanish | LILACS | ID: lil-152929

ABSTRACT

Presentamos un caso de un paciente que sufre politraumatismo, incluyendo un trauma raquimedular con paraplejia con nivel motor T9 y traumatismo torácico predominante unilateral con atelectasia masiva del pulmón izquierdo, refractaria al tratamiento habitual, incluyendo ventilación mecánica con PEEP que respondió favorablemente a la aplicación de ventilación mecánica diferencial asincrónica. Este es un método si bien, excepcional, que puede ser de franca utilidad en la resolución terapéutica de patología pulmonar unilateral como en nuestro caso


Subject(s)
Humans , Male , Adult , Respiration, Artificial/methods , Thoracic Injuries/therapy , Hemodynamics/physiology , Pulmonary Gas Exchange/physiology
17.
Virology ; 182(1): 8-16, 1991 May.
Article in English | MEDLINE | ID: mdl-1850914

ABSTRACT

We studied the post-translational modification of NS26, the protein product of rotavirus gene 11 segment. Based on the presence of a putative N-glycosylation site and the high content of serine and threonine residues in gene 11 amino acid sequence we investigated whether NS26 is modified by carbohydrate addition. Specific antibodies raised against the gene 11 product expressed in Escherichia coli recognized in infected cells two polypeptides with apparent molecular weight of 26,000 (26-kDa polypeptide) and 28,000 (28-kDa polypeptide). Pulse-chase experiments demonstrated that the 26-kDa product was processed to the 28-kDa polypeptide. Both polypeptides were metabolically labeled with [3H]glucosamine, indicating the presence of a carbohydrate moiety on the protein. NS26 was found to be resistant to endo-beta-N-acetylglucosaminidase H and endo-beta-N-acetylglucosaminidase F/peptide:N-glycosidase F treatment, but sensitive to removal by alkali-induced beta-elimination, suggesting that the saccharide chain was attached to the protein via an O-glycosidic linkage. Chromatographic analysis of total acid hydrolysates of [3H]glucosamine-labeled NS26-bound carbohydrate indicated the presence of N-acetylglucosamine. In addition, mild alkaline treatment of NS26 in the presence of NaB3H4 identified the O-linked carbohydrate moiety as N-acetylglucosamine. Taken together, these data demonstrate that NS26 is processed to a 28-kDa polypeptide by addition of O-linked monosaccharide residues of N-acetylglucosamine.


Subject(s)
Acetylglucosamine/metabolism , Capsid/metabolism , Rotavirus/metabolism , Viral Core Proteins/metabolism , Capsid/chemistry , Capsid/immunology , Cloning, Molecular , Glycoside Hydrolases/metabolism , Glycosylation , Molecular Weight , Precipitin Tests , Protein Processing, Post-Translational , Recombinant Proteins/metabolism , Viral Core Proteins/chemistry , Viral Core Proteins/immunology , Viral Nonstructural Proteins
18.
Bol Med Hosp Infant Mex ; 47(11): 737-45, 1990 Nov.
Article in Spanish | MEDLINE | ID: mdl-2285461

ABSTRACT

Peripheral pancytopenia is a syndrome which allows for an early diagnosis, and although is may cover a large number of pathological entities, it can be clearly defined into three groups of illnesses which evolve with this syndromal manifestations. The first group includes non-neoplastic illnesses which include aplastic anemia, hemophagocytic syndrome associated to infection, immunological diseases and the deficiency of folates or vitamin B12. The second group includes neoplastic diseases as acute leukemia, non-Hodgkin lymphoma, and Hodgkin's lymphoma with myelofibrosis, malignant histiocytosis and non-hematological neoplasms, like the neuroblastoma and the embryonal rhabdomyosarcoma. The third group is formed by illnesses which have some similarity with neoplasms.


Subject(s)
Pancytopenia/etiology , Anemia, Aplastic/complications , Folic Acid Deficiency/complications , Histiocytosis/complications , Humans , Neoplasms/complications , Neural Tube Defects/complications , Pancytopenia/diagnosis , Pancytopenia/immunology , Vitamin B 12 Deficiency/complications
19.
J Neurosci Methods ; 30(3): 185-7, 1989 Dec.
Article in English | MEDLINE | ID: mdl-2607780

ABSTRACT

A system for autoregulation of body temperature of large and small animals is described. The device uses the IC AD590 as a temperature transducer. It operates on the basis of continuous regulation of the heating current, and does not emit transients which interfere with electrical recordings. A panel meter shows either the rectal temperature of the animal or the current flow to the blanket.


Subject(s)
Body Temperature Regulation , Hot Temperature , Thermometers , Electronics
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