Your browser doesn't support javascript.
loading
Show: 20 | 50 | 100
Results 1 - 14 de 14
Filter
Add more filters











Publication year range
1.
Lipids Health Dis ; 19(1): 205, 2020 Sep 14.
Article in English | MEDLINE | ID: mdl-32921312

ABSTRACT

BACKGROUND AND AIMS: Diabetic kidney disease (DKD) is associated with lipid derangements that worsen kidney function and enhance cardiovascular (CVD) risk. The management of dyslipidemia, hypertension and other traditional risk factors does not completely prevent CVD complications, bringing up the participation of nontraditional risk factors such as advanced glycation end products (AGEs), carbamoylation and changes in the HDL proteome and functionality. The HDL composition, proteome, chemical modification and functionality were analyzed in nondialysis subjects with DKD categorized according to the estimated glomerular filtration rate (eGFR) and urinary albumin excretion rate (AER). METHODS: Individuals with DKD were divided into eGFR> 60 mL/min/1.73 m2 plus AER stages A1 and A2 (n = 10) and eGFR< 60 plus A3 (n = 25) and matched by age with control subjects (eGFR> 60; n = 8). RESULTS: Targeted proteomic analyses quantified 28 proteins associated with HDL in all groups, although only 2 were more highly expressed in the eGFR< 60 + A3 group than in the controls: apolipoprotein D (apoD) and apoA-IV. HDL from the eGFR< 60 + A3 group presented higher levels of total AGEs (20%), pentosidine (6.3%) and carbamoylation (4.2 x) and a reduced ability to remove 14C-cholesterol from macrophages (33%) in comparison to HDL from controls. The antioxidant role of HDL (lag time for LDL oxidation) was similar among groups, but HDL from the eGFR< 60 + A3 group presented a greater ability to inhibit the secretion of IL-6 and TNF-alpha (95%) in LPS-elicited macrophages in comparison to the control group. CONCLUSION: The increase in apoD and apoA-IV could contribute to counteracting the HDL chemical modification by AGEs and carbamoylation, which contributes to HDL loss of function in well-established DKD.


Subject(s)
Apolipoproteins A/blood , Apolipoproteins D/blood , Diabetic Nephropathies/blood , Lipoproteins, HDL/blood , Proteome/metabolism , Aged , Aged, 80 and over , Albuminuria/blood , Albuminuria/genetics , Albuminuria/pathology , Apolipoproteins A/genetics , Apolipoproteins D/genetics , Arginine/analogs & derivatives , Arginine/blood , Arginine/genetics , Case-Control Studies , Diabetic Nephropathies/genetics , Diabetic Nephropathies/pathology , Female , Gene Expression , Glomerular Filtration Rate , Glycation End Products, Advanced/blood , Glycation End Products, Advanced/genetics , Humans , Interleukin-6/genetics , Interleukin-6/metabolism , Kidney/metabolism , Kidney/pathology , Lipopolysaccharides/pharmacology , Lipoproteins, HDL/genetics , Lysine/analogs & derivatives , Lysine/blood , Lysine/genetics , Macrophages/drug effects , Macrophages/metabolism , Macrophages/pathology , Male , Middle Aged , Primary Cell Culture , Protein Carbamylation , Proteome/classification , Proteome/genetics , Renal Dialysis , Risk Factors , Tumor Necrosis Factor-alpha/genetics , Tumor Necrosis Factor-alpha/metabolism
2.
Braz J Med Biol Res ; 53(1): e9001, 2020.
Article in English | MEDLINE | ID: mdl-31939598

ABSTRACT

Due to its various structures in bio-compounds, snake venom is the indisputable result of evolutionary stages of molecules with an increasingly complex structure, high specificity, and of great importance for medicine because of their potential. The present study proposed an underpinning examination of venom composition from nine species of venomous snakes using a useful and replicable methodology. The objective was the extension of the evaluation of protein fractions in the field up to 230 kDa to permit possible identification of some fractions that are insufficiently studied. The gel capillary electrophoresis method on the chip was performed using an Agilent 2100 bioassay with the 80 and 230-LabChip Protein kits. Interpretation of electrophoresis was performed using the Protein 2100 expert (Agilent) test software as follows: a) Protein 80 (peak size scale): 1.60, 3.5, 6.50, 15.00, 28.00, 46.00, 63.00, 95.00 kDa; b) Protein 230 (peak size scale): 4.50, 7.00, 15.00, 28.00, 46.00, 63.00, 95.00, 150.00, 240.00 kDa. The screening revealed the presence of compounds with a molecular weight greater than 80 kDa, in the case of Vipera aspis and Vipera xantina palestinae. For V. aspis, a 125 kDa molecular weight pro-coagulant protein was identified, known as being involved in the reduction of plasma clotting time without any direct activity in the fibrinogen coagulation process. The samples examined on the Protein 230-LabChip electrophoresis chip can be considered as a novelty with possible uses in medicine, requiring further approaches by advanced proteomics techniques to confirm the intimate structural features and biological properties of snake venoms.


Subject(s)
Proteins/chemistry , Viper Venoms/chemistry , Viperidae/classification , Animals , Electrophoresis, Capillary , Proteins/analysis , Proteins/isolation & purification , Proteome/chemistry , Proteome/classification , Proteomics/methods , Viper Venoms/analysis
3.
Rev. bras. pesqui. méd. biol ; Braz. j. med. biol. res;53(1): e9001, Jan. 2020. tab, graf
Article in English | LILACS | ID: biblio-1055477

ABSTRACT

Due to its various structures in bio-compounds, snake venom is the indisputable result of evolutionary stages of molecules with an increasingly complex structure, high specificity, and of great importance for medicine because of their potential. The present study proposed an underpinning examination of venom composition from nine species of venomous snakes using a useful and replicable methodology. The objective was the extension of the evaluation of protein fractions in the field up to 230 kDa to permit possible identification of some fractions that are insufficiently studied. The gel capillary electrophoresis method on the chip was performed using an Agilent 2100 bioassay with the 80 and 230-LabChip Protein kits. Interpretation of electrophoresis was performed using the Protein 2100 expert (Agilent) test software as follows: a) Protein 80 (peak size scale): 1.60, 3.5, 6.50, 15.00, 28.00, 46.00, 63.00, 95.00 kDa; b) Protein 230 (peak size scale): 4.50, 7.00, 15.00, 28.00, 46.00, 63.00, 95.00, 150.00, 240.00 kDa. The screening revealed the presence of compounds with a molecular weight greater than 80 kDa, in the case of Vipera aspis and Vipera xantina palestinae. For V. aspis, a 125 kDa molecular weight pro-coagulant protein was identified, known as being involved in the reduction of plasma clotting time without any direct activity in the fibrinogen coagulation process. The samples examined on the Protein 230-LabChip electrophoresis chip can be considered as a novelty with possible uses in medicine, requiring further approaches by advanced proteomics techniques to confirm the intimate structural features and biological properties of snake venoms.


Subject(s)
Animals , Viper Venoms/chemistry , Proteins/chemistry , Viperidae/classification , Viper Venoms/analysis , Proteins/isolation & purification , Proteins/analysis , Electrophoresis, Capillary , Proteome/classification , Proteome/chemistry , Proteomics/methods
4.
Mar Biotechnol (NY) ; 21(1): 99-110, 2019 Feb.
Article in English | MEDLINE | ID: mdl-30456696

ABSTRACT

Total lipids and docosahexaenoic acid (DHA) production by a Chilean isolated thraustochytrid were evaluated under different growth conditions in shake flasks. The analyzed strain was identified as Thraustochytrium striatum according to an 18S rRNA gene sequence analysis. The strain (T. striatum AL16) showed negligible growth in media prepared with artificial seawater at concentrations lower than 50% v/v and pH lower than 5. Maltose and starch were better carbon sources for growth than glucose. DHA content of the biomass grown with maltose (60 g L-1) was doubled by increasing the agitation rate from 150 to 250 rpm. The DHA (0.8-6%) and eicosapentaenoic acid (0.2-21%) content in the total lipids varied depending on culture conditions and culture age. Lipid and DHA concentration increased (up to 5 g L-1 and 66 mg L-1, respectively) by regularly feeding the culture with a concentrated starch solution. Carotenoid accumulation was detected in cells grown with maltose or starch. Contrasting conditions of starch and glucose cultures were selected for comparative proteomics. Total protein extracts were separated by two-dimensional gel electrophoresis; 25 spots were identified using ESI-MS/MS. A protein database (143,006 entries) for proteomic interrogation was generated using de novo assembling of Thraustochytrium sp. LLF1b - MMETSP0199_2 transcriptome; 18 proteins differentially expressed were identified. Three ATP synthases were differentially accumulated in cultures with glucose, whereas malate dehydrogenase was more abundant in cells cultured with starch.


Subject(s)
Algal Proteins/genetics , Culture Media/pharmacology , Docosahexaenoic Acids/biosynthesis , Eicosapentaenoic Acid/biosynthesis , Proteome/genetics , Stramenopiles/drug effects , Algal Proteins/classification , Algal Proteins/isolation & purification , Biomass , Carotenoids/biosynthesis , Carotenoids/isolation & purification , Culture Media/chemistry , Docosahexaenoic Acids/isolation & purification , Eicosapentaenoic Acid/isolation & purification , Gene Expression , Gene Ontology , Glucose/metabolism , Glucose/pharmacology , Hydrogen-Ion Concentration , Maltose/metabolism , Maltose/pharmacology , Molecular Sequence Annotation , Proteome/classification , Proteome/isolation & purification , RNA, Ribosomal, 18S/genetics , Seawater/chemistry , Sequence Analysis, DNA , Starch/metabolism , Starch/pharmacology , Stramenopiles/genetics , Stramenopiles/growth & development , Stramenopiles/metabolism
5.
J Proteome Res ; 17(3): 961-977, 2018 03 02.
Article in English | MEDLINE | ID: mdl-29301397

ABSTRACT

Rhomboids are conserved intramembrane serine proteases involved in cell signaling processes. Their role in prokaryotes is scarcely known and remains to be investigated in Archaea. We previously constructed a rhomboid homologue deletion mutant (ΔrhoII) in Haloferax volcanii, which showed reduced motility, increased novobiocin sensitivity, and an N- glycosylation defect. To address the impact of rhoII deletion on H. volcanii physiology, the proteomes of mutant and parental strains were compared by shotgun proteomics. A total of 1847 proteins were identified (45.8% of H. volcanii predicted proteome), from which 103 differed in amount. Additionally, the mutant strain evidenced 99 proteins with altered electrophoretic migration, which suggested differential post-translational processing/modification. Integral membrane proteins that evidenced variations in concentration, electrophoretic migration, or semitryptic cleavage in the mutant were considered as potential RhoII targets. These included a PrsW protease homologue (which was less stable in the mutant strain), a predicted halocyanin, and six integral membrane proteins potentially related to the mutant glycosylation (S-layer glycoprotein, Agl15) and cell adhesion/motility (flagellin1, HVO_1153, PilA1, and PibD) defects. This study investigated for the first time the impact of a rhomboid protease on the whole proteome of an organism.


Subject(s)
Archaeal Proteins/genetics , Gene Deletion , Gene Expression Regulation, Archaeal , Haloferax volcanii/genetics , Protein Processing, Post-Translational , Proteome/genetics , Archaeal Proteins/classification , Archaeal Proteins/isolation & purification , Archaeal Proteins/metabolism , Bacterial Outer Membrane Proteins/genetics , Bacterial Outer Membrane Proteins/metabolism , Cell Adhesion , DNA-Binding Proteins/deficiency , DNA-Binding Proteins/genetics , Endopeptidases/deficiency , Endopeptidases/genetics , Gene Ontology , Glycosylation , Haloferax volcanii/chemistry , Haloferax volcanii/metabolism , Membrane Proteins/deficiency , Membrane Proteins/genetics , Metalloproteins/genetics , Metalloproteins/metabolism , Molecular Sequence Annotation , Proteome/classification , Proteome/isolation & purification , Proteome/metabolism , Spectrometry, Mass, Electrospray Ionization , Substrate Specificity
6.
PLoS One ; 11(1): e0145343, 2016.
Article in English | MEDLINE | ID: mdl-26731728

ABSTRACT

Puccinia psidii sensu lato (s.l.) is the causal agent of eucalyptus and guava rust, but it also attacks a wide range of plant species from the myrtle family, resulting in a significant genetic and physiological variability among populations accessed from different hosts. The uredospores are crucial to P. psidii dissemination in the field. Although they are important for the fungal pathogenesis, their molecular characterization has been poorly studied. In this work, we report the first in-depth proteomic analysis of P. psidii s.l. uredospores from two contrasting populations: guava fruits (PpGuava) and eucalyptus leaves (PpEucalyptus). NanoUPLC-MSE was used to generate peptide spectra that were matched to the UniProt Puccinia genera sequences (UniProt database) resulting in the first proteomic analysis of the phytopathogenic fungus P. psidii. Three hundred and fourty proteins were detected and quantified using Label free proteomics. A significant number of unique proteins were found for each sample, others were significantly more or less abundant, according to the fungal populations. In PpGuava population, many proteins correlated with fungal virulence, such as malate dehydrogenase, proteossomes subunits, enolases and others were increased. On the other hand, PpEucalyptus proteins involved in biogenesis, protein folding and translocation were increased, supporting the physiological variability of the fungal populations according to their protein reservoirs and specific host interaction strategies.


Subject(s)
Basidiomycota/metabolism , Basidiomycota/pathogenicity , Eucalyptus/microbiology , Proteomics/methods , Psidium/microbiology , Spores, Fungal/metabolism , Basidiomycota/classification , Chromatography, Liquid/methods , Fungal Proteins/classification , Fungal Proteins/metabolism , Host Specificity , Mass Spectrometry/methods , Plant Diseases/microbiology , Plant Leaves/microbiology , Proteome/classification , Proteome/metabolism , Species Specificity , Virulence
7.
J Proteomics ; 105: 323-39, 2014 Jun 13.
Article in English | MEDLINE | ID: mdl-24576642

ABSTRACT

In spite of its small territory of ~50,000km(2), Costa Rica harbors a remarkably rich biodiversity. Its herpetofauna includes 138 species of snakes, of which sixteen pit vipers (family Viperidae, subfamily Crotalinae), five coral snakes (family Elapidae, subfamily Elapinae), and one sea snake (Family Elapidae, subfamily Hydrophiinae) pose potential hazards to human and animal health. In recent years, knowledge on the composition of snake venoms has expanded dramatically thanks to the development of increasingly fast and sensitive analytical techniques in mass spectrometry and separation science applied to protein characterization. Among several analytical strategies to determine the overall protein/peptide composition of snake venoms, the methodology known as 'snake venomics' has proven particularly well suited and informative, by providing not only a catalog of protein types/families present in a venom, but also a semi-quantitative estimation of their relative abundances. Through a collaborative research initiative between Instituto de Biomedicina de Valencia (IBV) and Instituto Clodomiro Picado (ICP), this strategy has been applied to the study of venoms of Costa Rican snakes, aiming to obtain a deeper knowledge on their composition, geographic and ontogenic variations, relationships to taxonomy, correlation with toxic activities, and discovery of novel components. The proteomic profiles of venoms from sixteen out of the 22 species within the Viperidae and Elapidae families found in Costa Rica have been reported so far, and an integrative view of these studies is hereby presented. In line with other venomic projects by research groups focusing on a wide variety of snakes around the world, these studies contribute to a deeper understanding of the biochemical basis for the diverse toxic profiles evolved by venomous snakes. In addition, these studies provide opportunities to identify novel molecules of potential pharmacological interest. Furthermore, the establishment of venom proteomic profiles offers a fundamental platform to assess the detailed immunorecognition of individual proteins/peptides by therapeutic or experimental antivenoms, an evolving methodology for which the term 'antivenomics' was coined (as described in an accompanying paper in this special issue). BIOLOGICAL SIGNIFICANCE: Venoms represent an adaptive trait and an example of both divergent and convergent evolution. A deep understanding of the composition of venoms and of the principles governing the evolution of venomous systems is of applied importance for exploring the enormous potential of venoms as sources of chemical and pharmacological novelty but also to fight the consequences of snakebite envenomings. Key to this is the identification of evolutionary and ecological trends at different taxonomical levels. However, the evolution of venomous species and their venoms do not always follow the same course, and the identification of structural and functional convergences and divergences among venoms is often unpredictable by a phylogenetic hypothesis. Snake venomics is a proteomic-centered strategy to deconstruct the complex molecular phenotypes the venom proteomes. The proteomic profiles of venoms from sixteen out of the 22 venomous species within the Viperidae and Elapidae families found in Costa Rica have been completed so far. An integrative view of their venom composition, including the identification of geographic and ontogenic variations, is hereby presented. Venom proteomic profiles offer a fundamental platform to assess the detailed immunorecognition of individual venom components by therapeutic or experimental antivenoms. This aspect is reviewed in the companion paper. This article is part of a Special Issue entitled: Proteomics of non-model organisms.


Subject(s)
Proteome/chemistry , Proteome/classification , Proteomics/methods , Snake Venoms/chemistry , Snake Venoms/classification , Snakes , Animals , Costa Rica , Humans , Mass Spectrometry , Proteome/toxicity , Snake Venoms/toxicity
8.
J Proteome Res ; 11(2): 1152-62, 2012 Feb 03.
Article in English | MEDLINE | ID: mdl-22168127

ABSTRACT

Rear-fanged and aglyphous snakes are usually considered not dangerous to humans because of their limited capacity of injecting venom. Therefore, only a few studies have been dedicated to characterizing the venom of the largest parcel of snake fauna. Here, we investigated the venom proteome of the rear-fanged snake Thamnodynastes strigatus , in combination with a transcriptomic evaluation of the venom gland. About 60% of all transcripts code for putative venom components. A striking finding is that the most abundant type of transcript (∼47%) and also the major protein type in the venom correspond to a new kind of matrix metalloproteinase (MMP) that is unrelated to the classical snake venom metalloproteinases found in all snake families. These enzymes were recently suggested as possible venom components, and we show here that they are proteolytically active and probably recruited to venom from a MMP-9 ancestor. Other unusual proteins were suggested to be venom components: a protein related to lactadherin and an EGF repeat-containing transcript. Despite these unusual molecules, seven toxin classes commonly found in typical venomous snakes are also present in the venom. These results support the evidence that the arsenals of these snakes are very diverse and harbor new types of biologically important molecules.


Subject(s)
Colubridae/metabolism , Matrix Metalloproteinases/chemistry , Proteome/chemistry , Proteomics/methods , Snake Venoms/chemistry , Amino Acid Sequence , Animals , Matrix Metalloproteinases/classification , Molecular Sequence Data , Phylogeny , Protein Binding , Proteome/classification , Sequence Alignment , Snake Venoms/antagonists & inhibitors , Snake Venoms/classification , Snake Venoms/metabolism , Transcriptome
9.
J Proteome Res ; 11(1): 189-205, 2012 Jan 01.
Article in English | MEDLINE | ID: mdl-21970549

ABSTRACT

Iron is essential and ubiquitous in living organisms. The competition for this micronutrient between the host and its pathogens has been related to disease establishment. Cryptococcus gattii is an encapsulated yeast that causes cryptococcosis mainly in immunocompetent individuals. In this study, we analyzed the proteomic profile of the C. gattii R265 Vancouver Island isolate under iron-depleted and -repleted conditions by multidimensional protein identification technology (MudPIT) and by 2D-GE. Proteins and key mechanisms affected by alteration of iron levels such as capsule production, cAMP-signaling pathway, response to stress, and metabolic pathways related to mitochondrial function were identified. Our results also show both proteomic methodologies employed to be complementary.


Subject(s)
Cryptococcus gattii/metabolism , Fungal Proteins/metabolism , Iron/physiology , Proteome/metabolism , Biosynthetic Pathways , Cryptococcus gattii/genetics , Cryptococcus gattii/growth & development , Electrophoresis, Gel, Two-Dimensional , Fungal Proteins/classification , Fungal Proteins/genetics , Gene Expression , Gene Expression Regulation, Fungal , Iron/metabolism , Molecular Sequence Annotation , Proteome/classification , Proteome/genetics , Proteomics
10.
BMC Genomics ; 12: 215, 2011 May 06.
Article in English | MEDLINE | ID: mdl-21548963

ABSTRACT

BACKGROUND: Schistosomiasis remains an important parasitic disease and a major economic problem in many countries. The Schistosoma mansoni genome and predicted proteome sequences were recently published providing the opportunity to identify new drug candidates. Eukaryotic protein kinases (ePKs) play a central role in mediating signal transduction through complex networks and are considered druggable targets from the medical and chemical viewpoints. Our work aimed at analyzing the S. mansoni predicted proteome in order to identify and classify all ePKs of this parasite through combined computational approaches. Functional annotation was performed mainly to yield insights into the parasite signaling processes relevant to its complex lifestyle and to select some ePKs as potential drug targets. RESULTS: We have identified 252 ePKs, which corresponds to 1.9% of the S. mansoni predicted proteome, through sequence similarity searches using HMMs (Hidden Markov Models). Amino acid sequences corresponding to the conserved catalytic domain of ePKs were aligned by MAFFT and further used in distance-based phylogenetic analysis as implemented in PHYLIP. Our analysis also included the ePK homologs from six other eukaryotes. The results show that S. mansoni has proteins in all ePK groups. Most of them are clearly clustered with known ePKs in other eukaryotes according to the phylogenetic analysis. None of the ePKs are exclusively found in S. mansoni or belong to an expanded family in this parasite. Only 16 S. mansoni ePKs were experimentally studied, 12 proteins are predicted to be catalytically inactive and approximately 2% of the parasite ePKs remain unclassified. Some proteins were mentioned as good target for drug development since they have a predicted essential function for the parasite. CONCLUSIONS: Our approach has improved the functional annotation of 40% of S. mansoni ePKs through combined similarity and phylogenetic-based approaches. As we continue this work, we will highlight the biochemical and physiological adaptations of S. mansoni in response to diverse environments during the parasite development, vector interaction, and host infection.


Subject(s)
Protein Kinases/classification , Protein Kinases/metabolism , Proteomics , Schistosoma mansoni/enzymology , Schistosoma mansoni/parasitology , Animals , Catalytic Domain , Markov Chains , Phylogeny , Protein Kinases/chemistry , Proteome/chemistry , Proteome/classification , Proteome/metabolism , Schistosoma mansoni/cytology , Signal Transduction
11.
J Proteome Res ; 9(10): 5473-83, 2010 Oct 01.
Article in English | MEDLINE | ID: mdl-20804217

ABSTRACT

CIGB-300 is a proapoptotic peptide-based drug that abrogates the CK2-mediated phosphorylation. This peptide has antineoplastic effect on lung cancer cells in vitro and in vivo. To understand the mechanisms involved on such anticancer activity, the NCI-H125 cell line proteomic profile after short-term incubation (45 min) with CIGB-300 was investigated. As determined by 2-DE or 2D-LC-MS/MS, 137 proteins changed their abundances more than 2-fold in response to the CIGB-300 treatment. The expression levels of proteins related to ribosome biogenesis, metastasis, cell survival and proliferation, apoptosis, and drug resistance were significantly modulated by the presence of CIGB-300. The protein translation process was the most affected (23% of the identified proteins). From the proteome analysis of the NCI-H125 cell line, novel potentialities for CIGB-300 as anticancer agent were evidenced.


Subject(s)
Peptides, Cyclic/pharmacology , Protein Biosynthesis/drug effects , Proteome/analysis , Proteomics/methods , Antineoplastic Agents/pharmacology , Apoptosis/drug effects , Carcinoma, Non-Small-Cell Lung/metabolism , Carcinoma, Non-Small-Cell Lung/pathology , Cell Line, Tumor , Cell Proliferation/drug effects , Cell Survival/drug effects , Chromatography, Liquid , Cluster Analysis , Electrophoresis, Gel, Two-Dimensional , Humans , Lung Neoplasms/metabolism , Lung Neoplasms/pathology , Mass Spectrometry , Proteome/classification
12.
Tuberculosis (Edinb) ; 89(2): 126-35, 2009 Mar.
Article in English | MEDLINE | ID: mdl-19231290

ABSTRACT

To contribute to Mycobacterium bovis BCG characterization, two substrains were analyzed using two-dimensional gel electrophoresis (2D-PAGE) and mass spectrometry (MS), based on their protective efficacy in a pulmonary-tuberculosis mouse model. Cell-fraction proteins of BCG Denmark and Phipps substrains were separated into approximately 500 spots in 2D-PAGE. The proteomes were similar in protein number, and isoelectric point (pI) and molecular mass (MM) distribution. Statistical analysis, resulted in 72 spots with no change, and 168 and 90 unique for BCG Phipps or Denmark, respectively. Two hundred and fourteen spots showed changes in intensity of >1-fold, 138 of Denmark, and 76 of Phipps. Seventeen spots were selected for MS-based identification (13 from Phipps and 4 from Denmark), including unique, as well as proteins with changes in intensity. The proteins identified participate in virulence, detoxification, adaptation, lipid metabolism, information pathways, cell wall and cell processes, intermediary metabolism and respiration, or still hypotheticals. Our findings contribute to phenotype characterization of BCG substrains and provide new elements to consider for the design of diagnostic tools, drug targets and a new vaccine against tuberculosis based upon protein expression through quantitative statistical analysis.


Subject(s)
BCG Vaccine/chemistry , Mycobacterium bovis/classification , Proteome/classification , Animals , BCG Vaccine/classification , Bacterial Proteins/analysis , Bacterial Proteins/genetics , Bacterial Proteins/physiology , Electrophoresis, Gel, Two-Dimensional/methods , Humans , Mice , Mycobacterium bovis/chemistry , Mycobacterium bovis/genetics , Proteomics/methods , Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization/methods
13.
FEBS Lett ; 580(18): 4417-22, 2006 Aug 07.
Article in English | MEDLINE | ID: mdl-16857193

ABSTRACT

We investigated the putative toxins of Philodryas olfersii (Colubridae), a representative of a family of snakes neglected in venom studies despite their growing medical importance. Transcriptomic data of the venom gland complemented by proteomic analysis of the gland secretion revealed the presence of major toxin classes from the Viperidae family, including serine proteases, metalloproteases, C-type lectins, Crisps, and a C-type natriuretic peptide (CNP). Interestingly, the phylogenetic analysis of the CNP precursor showed it as a linker between two related precursors found in Viperidae and Elapidae snakes. We suggest that these precursors constitute a monophyletic group derived from the vertebrate CNPs.


Subject(s)
Colubridae/classification , Snake Venoms/classification , Amino Acid Sequence , Animals , Colubridae/genetics , Colubridae/metabolism , Elapidae/classification , Evolution, Molecular , Expressed Sequence Tags/chemistry , Female , Lectins, C-Type/analysis , Lectins, C-Type/chemistry , Lectins, C-Type/genetics , Male , Metalloproteases/analysis , Metalloproteases/chemistry , Metalloproteases/genetics , Molecular Sequence Data , Natriuretic Peptides/chemistry , Natriuretic Peptides/classification , Natriuretic Peptides/genetics , Oligopeptides/chemistry , Oligopeptides/classification , Oligopeptides/genetics , Phylogeny , Protein Precursors/chemistry , Protein Precursors/classification , Protein Precursors/genetics , Proteome/chemistry , Proteome/classification , Proteome/genetics , Sequence Alignment , Serine Endopeptidases/analysis , Serine Endopeptidases/chemistry , Serine Endopeptidases/genetics , Snake Venoms/chemistry , Snake Venoms/genetics , Transcription, Genetic , Viperidae/classification
14.
FEBS Letters ; 580(18): 4417-4422, Jul 13, 2006.
Article in English | Sec. Est. Saúde SP, SESSP-IBPROD, Sec. Est. Saúde SP, SESSP-IBACERVO | ID: biblio-1062802

ABSTRACT

We investigated the putative toxins of Philodryas olfersii (Colubridae), a representative of a family of snakes neglected in venom studies despite their growing medical importance. Transcriptomic data of the venom gland complemented by proteomic analysis of the gland secretion revealed the presence of major toxin classes from the Viperidae family, including serine proteases, metalloproteases, C-type lectins, Crisps, and a C-type natriuretic peptide (CNP). Interestingly, the phylogenetic analysis of the CNP precursor showed it as a linker between two related precursors found in Viperidae and Elapidae snakes. We suggest that these precursors constitute a monophyletic group derived from the vertebrate CNPs.


Subject(s)
Animals , Colubridae/classification , Colubridae/metabolism , Proteome/classification , Proteome/chemistry , Snake Venoms/analysis , Molecular Sequence Data , Lectins, C-Type/analysis , Lectins, C-Type/chemistry , Oligopeptides/genetics , Oligopeptides/chemistry , Serine Endopeptidases/analysis , Serine Endopeptidases/chemistry
SELECTION OF CITATIONS
SEARCH DETAIL