Your browser doesn't support javascript.
loading
Show: 20 | 50 | 100
Results 1 - 6 de 6
Filter
Add more filters











Database
Language
Publication year range
1.
Science ; 363(6423)2019 01 11.
Article in English | MEDLINE | ID: mdl-30630897

ABSTRACT

The Hansen et al critique centers on the lack of spatial agreement between two very different datasets. Nonetheless, properly constructed comparisons designed to reconcile the two datasets yield up to 90% agreement (e.g., in South America).


Subject(s)
Carbon/analysis , Tropical Climate , Biomass , Forests , South America
2.
FEMS Microbiol Lett ; 198(1): 31-6, 2001 Apr 20.
Article in English | MEDLINE | ID: mdl-11325550

ABSTRACT

To identify antigens that would improve the accuracy of serological diagnosis of active tuberculosis, we cloned the genes encoding nine potentially immunogenic secreted or surface-associated proteins of Mycobacterium tuberculosis. Recombinant proteins were reacted with sera from HIV-negative individuals with extrapulmonary tuberculosis (EP-TB) or HIV-positive individuals with pulmonary tuberculosis (TBH). Specific and high level antibody responses were obtained for four recombinant proteins, of which antigen GST-822 was recognized by 60% of EP-TB and 42% of TBH and antigen MBP-506 was recognized by 45% of EP-TB and 61% of TBH. These results suggest that these proteins are strong candidates as subunits in a polyvalent serodiagnostic test.


Subject(s)
Antibodies, Bacterial/blood , Antigens, Bacterial/immunology , Enzyme-Linked Immunosorbent Assay , Mycobacterium tuberculosis/immunology , Tuberculosis/diagnosis , Antigens, Bacterial/genetics , Bacterial Proteins/genetics , Bacterial Proteins/immunology , Cloning, Molecular , Genes, Bacterial , Humans , Mycobacterium tuberculosis/genetics , Open Reading Frames , Polymerase Chain Reaction , Recombinant Fusion Proteins/immunology , Recombinant Fusion Proteins/metabolism
3.
Nature ; 403(6767): 301-4, 2000 Jan 20.
Article in English | MEDLINE | ID: mdl-10659847

ABSTRACT

The distribution of sources and sinks of carbon among the world's ecosystems is uncertain. Some analyses show northern mid-latitude lands to be a large sink, whereas the tropics are a net source; other analyses show the tropics to be nearly neutral, whereas northern mid-latitudes are a small sink. Here we show that the annual flux of carbon from deforestation and abandonment of agricultural lands in the Brazilian Amazon was a source of about 0.2 Pg Cyr(-1) over the period 1989-1998 (1 Pg is 10(15) g). This estimate is based on annual rates of deforestation and spatially detailed estimates of deforestation, regrowing forests and biomass. Logging may add another 5-10% to this estimate, and fires may double the magnitude of the source in years following a drought. The annual source of carbon from land-use change and fire approximately offsets the sink calculated for natural ecosystems in the region. Thus this large area of tropical forest is nearly balanced with respect to carbon, but has an interannual variability of +/- 0.2 PgC yr(-1).


Subject(s)
Carbon/metabolism , Conservation of Natural Resources , Ecosystem , Trees , Atmosphere , Biomass , Brazil
4.
J Infect Dis ; 181(1): 325-30, 2000 Jan.
Article in English | MEDLINE | ID: mdl-10608782

ABSTRACT

A tetrapeptide and a recombinant protein, each representing 4 immunodominant epitopes of Trypanosoma cruzi, were tested by use of ELISA for the detection of serum antibodies. Sera from individuals with Chagas' disease, including persons untreated and successfully or unsuccessfully treated, were tested. These assays detected antibody in 100% of the parasitemias. The antibody reactivity decreased based on the success of treatment. Higher sensitivity was observed for tetrapeptide/recombinant protein assays than for lysate-based ELISA, and specificity was improved, particularly with Leishmania sera. The results indicate that multiepitope antigens provide a more sensitive and specific alternative to lysate for detection of anti-T. cruzi antibodies, as required for developing blood screening assays.


Subject(s)
Antibodies, Protozoan/blood , Chagas Disease/diagnosis , Enzyme-Linked Immunosorbent Assay/methods , Oligopeptides , Recombinant Proteins , Brazil/epidemiology , Humans , Immunodominant Epitopes , Parasitemia/diagnosis , Reproducibility of Results , Sensitivity and Specificity
5.
Trans R Soc Trop Med Hyg ; 93(6): 603-6, 1999.
Article in English | MEDLINE | ID: mdl-10717744

ABSTRACT

An enzyme-linked immunosorbent assay (ELISA) has been developed to detect IgG and IgM antibodies in human sera against a synthetic tripeptide derived from a hybrid peptide containing 3 specific epitopes from Trypanosoma cruzi. This assay was compared in Brazil with one using conventional antigen, the alkaline crude extract. Serum samples were divided into positive (40 samples) or negative (107 samples) for Chagas disease. Positive samples included 9 serum samples from patients with acute Chagas disease, while negative samples included 57 samples from patients suffering from viral diseases. The total percentages of IgG positive samples from patients with chronic Chagas disease for alkaline extract and synthetic tripeptide were 93.5% and 100%, respectively. All samples from patients with acute Chagas disease were confirmed positive for IgM antibodies by using both the tripeptide and the alkaline extract. However, the results for anti-T. cruzi IgM in the group of chronic Chagas disease patients demonstrated that 41.9% were positive for IgM with the alkaline extract, while the synthetic peptide showed a significantly lower number of positive samples (12.9%). The serum samples from healthy people showed similar results for both antigens. However, 40% of the serum samples from patients presenting with viral diseases were IgM positive for Chagas disease when assayed with conventional antigen; with the synthetic tripeptide as antigen, 100% of this group of samples were found to be negative. Thus, as the results of ELISA with synthetic tripeptide showed higher rates of sensitivity and specificity than ELISA with conventional antigen, the former should be included as a laboratory tool in the serodiagnosis of Chagas disease.


Subject(s)
Antibodies, Protozoan/blood , Antigens, Protozoan , Chagas Disease/diagnosis , Immunoglobulin G/blood , Immunoglobulin M/blood , Trypanosoma cruzi/immunology , Acute Disease , Animals , Antigens, Protozoan/chemistry , Antigens, Protozoan/immunology , Enzyme-Linked Immunosorbent Assay/methods , Epitopes/chemistry , Epitopes/immunology , Humans , Peptides/chemical synthesis , Peptides/immunology , Sensitivity and Specificity
6.
J Infect Dis ; 173(3): 758-61, 1996 Mar.
Article in English | MEDLINE | ID: mdl-8627048

ABSTRACT

The diagnosis of visceral leishmaniasis (VL), a serious and often fatal parasitic disease caused by members of the Leishmania donovani complex, remains problematic. Current methods rely on clinical criteria, parasite identification in aspirate material, and serology. The latter methods use crude antigen preparations lacking in specificity. A previously described cloned antigen, rK39, of Leishmania specific for all members of the L. donovani complex (L. chagasi, L. donovani, L. infantum) was very useful in the serodiagnosis by ELISA of both human and canine VL. The present study demonstrated that rK39 seroreactivity correlated with active disease. The sera from early or self-healing infected subjects reacted with leishmanial lysate and were generally nonreactive with rK39. These data demonstrate the utility of rK39 in the serodiagnosis of VL and as an indicator of active disease.


Subject(s)
Antibodies, Protozoan/blood , Antigens, Protozoan , Leishmania infantum/immunology , Leishmaniasis, Visceral/diagnosis , Leishmaniasis, Visceral/immunology , Protozoan Proteins/immunology , Animals , Antibody Specificity , Antigens, Protozoan/genetics , Biomarkers , Brazil/epidemiology , Child , Cloning, Molecular , Cross Reactions , Dogs , Enzyme-Linked Immunosorbent Assay , Humans , Leishmania infantum/genetics , Leishmaniasis, Visceral/epidemiology , Protozoan Proteins/genetics , Serologic Tests
SELECTION OF CITATIONS
SEARCH DETAIL