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1.
Braz J Infect Dis ; 25(4): 101604, 2021.
Article in English | MEDLINE | ID: mdl-34416142

ABSTRACT

BACKGROUND: São Paulo city has been one of the regions most affected by the COVID-19 pandemic in Brazil. Frequent asymptomatic and oligosymptomatic infections and poor access to diagnostic tests make serosurveys crucial to monitor the magnitude of the epidemic and to inform public health policies, such as vaccination plans. OBJECTIVES: To estimate, early in the epidemic, the seroprevalence of antibodies to SARS-CoV-2 in adults living in the six most affected districts in São Paulo city, and to assess potential associated risk factors. METHODS: This was a cross-sectional population-based survey of 1,152 households randomly selected from 72 census tracts. During the period May 4-12, 2020, 463 participants completed a questionnaire on sociodemographic characteristics and history of symptoms in the past two weeks, and provided a blood sample. Prevalence of SARS-CoV-2 antibodies was the outcome of interest and was estimated based on results of two immunoassays, Maglumi SARS-CoV-2 chemiluminescence assay Immunoglobulin (Ig) M (IgM) and IgG, and Roche electrochemiluminescence assay total Ig. Serum samples reactive to either assay were considered positive. RESULTS: Weighted overall seroprevalence was 6% (95%CI 3.9-8.3%). No association was observed between seropositivity and sex, age group or education level. Participants who reported black and brown skin color showed a 2.7 fold higher prevalence than people with white skin (p = 0.007). Among the 30 seropositive individuals, 14 (46.6%) reported no COVID-19 compatible symptoms in the past two weeks. CONCLUSION: This study represents the first assessment of SARS-CoV-2 seroprevalence in the city of São Paulo and 6% is the baseline estimate of a series of population-based seroprevalence surveys. Serological screening using sound serological assays is the key tool to monitoring temporal and geographic changes in the spread of the virus through an important epicenter of the COVID-19 pandemic in Brazil. Ultimately, it may inform prevention and control efforts.


Subject(s)
COVID-19 , SARS-CoV-2 , Adult , Antibodies, Viral , Brazil/epidemiology , Cross-Sectional Studies , Humans , Immunoglobulin G , Pandemics , Seroepidemiologic Studies
2.
Braz. j. infect. dis ; 25(4): 101604, 2021. tab, graf
Article in English | LILACS | ID: biblio-1339443

ABSTRACT

ABSTRACT Background: São Paulo city has been one of the regions most affected by the COVID-19 pandemic in Brazil. Frequent asymptomatic and oligosymptomatic infections and poor access to diagnostic tests make serosurveys crucial to monitor the magnitude of the epidemic and to inform public health policies, such as vaccination plans. Objectives: To estimate, early in the epidemic, the seroprevalence of antibodies to SARS-CoV-2 in adults living in the six most affected districts in São Paulo city, and to assess potential associated risk factors. Methods: This was a cross-sectional population-based survey of 1,152 households randomly selected from 72 census tracts. During the period May 4-12, 2020, 463 participants completed a questionnaire on sociodemographic characteristics and history of symptoms in the past two weeks, and provided a blood sample. Prevalence of SARS-CoV-2 antibodies was the outcome of interest and was estimated based on results of two immunoassays, Maglumi SARS-CoV-2 chemiluminescence assay Immunoglobulin (Ig) M (IgM) and IgG, and Roche electrochemiluminescence assay total Ig. Serum samples reactive to either assay were considered positive. Results: Weighted overall seroprevalence was 6% (95%CI 3.9-8.3%). No association was observed between seropositivity and sex, age group or education level. Participants who reported black and brown skin color showed a 2.7 fold higher prevalence than people with white skin (p = 0.007). Among the 30 seropositive individuals, 14 (46.6%) reported no COVID-19 compatible symptoms in the past two weeks. Conclusion: This study represents the first assessment of SARS-CoV-2 seroprevalence in the city of São Paulo and 6% is the baseline estimate of a series of population-based seroprevalence surveys. Serological screening using sound serological assays is the key tool to monitoring temporal and geographic changes in the spread of the virus through an important epicenter of the COVID-19 pandemic in Brazil. Ultimately, it may inform prevention and control efforts.


Subject(s)
Humans , Adult , SARS-CoV-2 , COVID-19 , Brazil/epidemiology , Immunoglobulin G , Seroepidemiologic Studies , Cross-Sectional Studies , Pandemics , Antibodies, Viral
3.
Trop Plant Biol ; 4(1): 62-89, 2011 Mar.
Article in English | MEDLINE | ID: mdl-21614128

ABSTRACT

Global interest in sugarcane has increased significantly in recent years due to its economic impact on sustainable energy production. Sugarcane breeding and better agronomic practices have contributed to a huge increase in sugarcane yield in the last 30 years. Additional increases in sugarcane yield are expected to result from the use of biotechnology tools in the near future. Genetically modified (GM) sugarcane that incorporates genes to increase resistance to biotic and abiotic stresses could play a major role in achieving this goal. However, to bring GM sugarcane to the market, it is necessary to follow a regulatory process that will evaluate the environmental and health impacts of this crop. The regulatory review process is usually accomplished through a comparison of the biology and composition of the GM cultivar and a non-GM counterpart. This review intends to provide information on non-GM sugarcane biology, genetics, breeding, agronomic management, processing, products and byproducts, as well as the current technologies used to develop GM sugarcane, with the aim of assisting regulators in the decision-making process regarding the commercial release of GM sugarcane cultivars.

4.
Virus Genes ; 32(3): 289-98, 2006 Jun.
Article in English | MEDLINE | ID: mdl-16732481

ABSTRACT

The Citrus leprosis disease (CiL) is associated to a virus (CiLV) transmitted by Brevipalpus spp. mites (Acari: Tenuipalpidae). CiL is endemic in Brazil and its recently spreading to Central America represents a threat to citrus industry in the USA. Electron microscopy images show two forms of CiLV: a rare nuclear form, characterized by rod-shaped naked particle (CiLV-N) and a common cytoplasmic form (CiLV-C) associated with bacilliform-enveloped particle and cytoplasmic viroplasm. Due to this morphological feature, CiLV-C has been treated as Rhabdovirus-like. In this paper we present the complete nucleotide sequence and genomic organization of CiLV-C. It is a bipartite virus with sequence similarity to ssRNA positive plant virus. RNA1 encodes a putative replicase polyprotein and an ORF with no known function. RNA2 encodes 4 ORFs. pl5, p24 and p61 have no significant similarity to any known proteins and p32 encodes a protein with similarity to a viral movement protein. The CiLV-C sequences are associated with typical symptoms of CiL by RT-PCR. Phylogenetic analysis suggests that CiLV-C is probably a member of a new family of plant virus evolutionarily related to Tobamovirus.


Subject(s)
Base Sequence , Citrus sinensis/virology , Genome, Viral , Plant Diseases/virology , Plant Viruses/genetics , RNA Viruses/genetics , Molecular Sequence Data , Phylogeny , Plant Leaves/virology , Plant Viruses/classification , RNA Viruses/classification , RNA, Viral/analysis , RNA, Viral/isolation & purification , Reverse Transcriptase Polymerase Chain Reaction , Sequence Analysis, DNA
5.
J Virol ; 79(5): 3028-37, 2005 Mar.
Article in English | MEDLINE | ID: mdl-15709023

ABSTRACT

Citrus sudden death (CSD) is a new disease that has killed approximately 1 million orange trees in Brazil. Here we report the identification of a new virus associated with the disease. RNAs isolated from CSD-affected and nonaffected trees were used to construct cDNA libraries. A set of viral sequences present exclusively in libraries of CSD-affected trees was used to obtain the complete genome sequence of the new virus. Phylogenetic analysis revealed that this virus is a new member of the genus Marafivirus. Antibodies raised against the putative viral coat proteins allowed detection of viral antigens of expected sizes in affected plants. Electron microscopy of purified virus confirmed the presence of typical isometric Marafivirus particles. The screening of 773 affected and nonaffected citrus trees for the presence of the virus showed a 99.7% correlation between disease symptoms and the presence of the virus. We also detected the virus in aphids feeding on affected trees. These results suggest that this virus is likely to be the causative agent of CSD. The virus was named Citrus sudden death-associated virus.


Subject(s)
Citrus/virology , Tymoviridae/genetics , Tymoviridae/isolation & purification , Amino Acid Sequence , Animals , Aphids/virology , Base Sequence , Brazil , Capsid Proteins/genetics , DNA, Viral/genetics , Genome, Viral , Microscopy, Electron , Molecular Sequence Data , Phylogeny , Plant Diseases/virology , Tymoviridae/classification , Tymoviridae/pathogenicity
6.
Eur J Biochem ; 270(14): 2937-44, 2003 Jul.
Article in English | MEDLINE | ID: mdl-12846826

ABSTRACT

The Ca2+-induced transition in the troponin complex (Tn) regulates vertebrate striated muscle contraction. Tn was reconstituted with recombinant forms of troponin I (TnI) containing a single intrinsic 5-hydroxytryptophan (5HW). Fluorescence analysis of these mutants of TnI demonstrate that the regions in TnI that respond to Ca2+ binding to the regulatory N-domain of TnC are the inhibitory region (residues 96-116) and a neighboring region that includes position 121. Our data confirms the role of TnI as a modulator of the Ca2+ affinity of TnC; we show that point mutations and incorporation of 5HW in TnI can affect both the affinity and the cooperativity of Ca2+ binding to TnC. We also discuss the possibility that the regulatory sites in the N-terminal domain of TnC might be the high affinity Ca2+-binding sites in the troponin complex.


Subject(s)
Calcium/pharmacology , Tropomyosin/physiology , Troponin I/physiology , Troponin/physiology , 5-Hydroxytryptophan/chemistry , 5-Hydroxytryptophan/metabolism , Allosteric Regulation , Binding Sites , Calcium/chemistry , Calcium/metabolism , Escherichia coli/genetics , Escherichia coli/metabolism , Mutagenesis, Site-Directed , Point Mutation/physiology , Protein Binding , Protein Conformation , Protein Structure, Tertiary , Recombinant Proteins/genetics , Recombinant Proteins/metabolism , Spectrometry, Fluorescence , Tropomyosin/metabolism , Troponin/metabolism , Troponin I/genetics , Troponin I/metabolism
7.
J Biol Chem ; 278(13): 11007-14, 2003 Mar 28.
Article in English | MEDLINE | ID: mdl-12531902

ABSTRACT

Calcium binding to chicken recombinant skeletal muscle TnC (TnC) and its mutants containing tryptophan (F29W), 5-hydroxytryptophan (F29HW), or 7-azatryptophan (F29ZW) at position 29 was measured by flow dialysis and by fluorescence. Comparative analysis of the results allowed us to determine the influence of each amino acid on the calcium binding properties of the N-terminal regulatory domain of the protein. Compared with TnC, the Ca(2+) affinity of N-terminal sites was: 1) increased 6-fold in F29W, 2) increased 3-fold in F29ZW, and 3) decreased slightly in F29HW. The Ca(2+) titration of F29ZW monitored by fluorescence displayed a bimodal curve related to sequential Ca(2+) binding to the two N-terminal Ca(2+) binding sites. Single and double mutants of TnC, F29W, F29HW, and F29ZW were constructed by replacing aspartate by alanine at position 30 (site I) or 66 (site II) or both. Ca(2+) binding data showed that the Asp --> Ala mutation at position 30 impairs calcium binding to site I only, whereas the Asp --> Ala mutation at position 66 impairs calcium binding to both sites I and II. Furthermore, the Asp --> Ala mutation at position 30 eliminates the differences in Ca(2+) affinity observed for replacement of Phe at position 29 by Trp, 5-hydroxytryptophan, or 7-azatryptophan. We conclude that position 29 influences the affinity of site I and that Ca(2+) binding to site I is dependent on the previous binding of metal to site II.


Subject(s)
Calcium/metabolism , Muscle, Skeletal/metabolism , Troponin C/metabolism , Animals , Base Sequence , Chickens , DNA Primers , Mutagenesis , Protein Binding , Recombinant Proteins/metabolism , Spectrometry, Fluorescence
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