RESUMO
An experimental and clinical study was carried out on 76 patients with implant-supported restorations in the posterior zones of the lower jaw, divided in two groups (with no signs of bone resorption around the implants and with resorption signs) and one control group. The results of the study allowed optimizing the angulation of dental implants, providing an opportunity for individual positioning of dental implant in the mandible depending on the direction of functional load.
Assuntos
Arco Dental/cirurgia , Implantes Dentários , Oclusão Dentária , Planejamento de Prótese Dentária/métodos , Prótese Dentária Fixada por Implante , Adolescente , Adulto , Feminino , Humanos , Masculino , Pessoa de Meia-Idade , Adulto JovemRESUMO
A total of 1107 fecal samples from young children admitted to hospital for acute enteric infection in January to December 2007 were tested for astroviruses. Astroviruses were detected in 64 (5.8%) of the 1107 stool samples, only 50% of them were found as monoinfections. Astroviruses were recorded throughout the year; however, no seasonality for this infection could be ascertained. Cases of astrovirus infection were mainly observed in infants under one year of age (90%). Astroviruses were typed sequencing the ORF2 fragment; only HAstV-1 and HAstV-2 were found in Novosibirsk.
Assuntos
Infecções por Astroviridae/epidemiologia , Mamastrovirus/genética , Infecções por Astroviridae/virologia , Sequência de Bases , Pré-Escolar , Fezes/virologia , Hospitais , Humanos , Lactente , Recém-Nascido , Mamastrovirus/classificação , Epidemiologia Molecular , Dados de Sequência Molecular , Fases de Leitura Aberta/genética , Linhagem , Estações do Ano , Sibéria , População UrbanaRESUMO
A recombinant pSC13D6 plasmid DNA was constructed based on cDNA fragments of genes encoding variable domains of heavy and light chains of the MKA 13D6 monoclonal antibody against glycoprotein of the tick-borne encephalitis (TBE) virus. This plasmid provided expression in Escherichia coli cells of the sc13D6 single-chain antibody against the TBE virus. The produced antibodies could bind to the TBE virus, strain 205, and the TBE virus recombinant E protein. The affinity constant of purified sc13D6 was (3.0 +/- 0.2) x 10(7) M(-1) for the equilibrium state and (2.8 +/- 0.3) x 10(7) M(-1) in the case of antigen-antibody formation on the surface. The obtained single-chain antibody could inhibit the infection potency of the TBE virus on a monolayer of eukaryotic cells. The calculated IC50 value for sc13D6 was 16.7 microg/ml.
Assuntos
Anticorpos Monoclonais/química , Anticorpos Neutralizantes/química , Vírus da Encefalite Transmitidos por Carrapatos/imunologia , Sequência de Aminoácidos , Anticorpos Monoclonais/genética , Anticorpos Monoclonais/isolamento & purificação , Anticorpos Neutralizantes/genética , Anticorpos Neutralizantes/isolamento & purificação , Afinidade de Anticorpos/imunologia , Cromatografia em Gel , Escherichia coli/genética , Immunoblotting , Dados de Sequência Molecular , Testes de Neutralização , Fragmentos de Peptídeos/química , Fragmentos de Peptídeos/genética , Fragmentos de Peptídeos/imunologia , Plasmídeos , Proteínas Recombinantes/química , Proteínas Recombinantes/genética , Proteínas Recombinantes/isolamento & purificaçãoRESUMO
Examination of 1898 patients with acute enteric infection from March 2005 to February 2007 showed that group A rotaviruses were the most frequent cause (35%) of acute gastroenteritis among children under 3 years of age. Majority of cases of rotavirus infection was detected in infants under 1 year of age (71.8%). The peak of sporadic incidence was observed between February and May. High rate of mixed infection (45.6%) was observed - associations of rotaviruses with other viruses (noroviruses, astroviruses) and bacteria (Salmonella, Shigella, enteroinvasive Escherichia coli, Campylobacter, and opportunistic species) were detected. P- and G-genotypes of 337(50.8%) isolates of group A rotaviruses were determined by RT-PCR. The most prevalent strain was P[8]G1 (54.6%) followed by P[8]G3 (10.7%), P[8]G9 (8.6%), P[4]G2 (8.3%), and P[8]G4 (4.5%) genotypes.
Assuntos
Diarreia Infantil/epidemiologia , Diarreia Infantil/virologia , Infecções por Rotavirus/epidemiologia , Infecções por Rotavirus/virologia , Rotavirus/classificação , Doença Aguda , Antígenos Virais/genética , Infecções por Astroviridae/epidemiologia , Infecções por Caliciviridae/epidemiologia , Infecções por Campylobacter/epidemiologia , Proteínas do Capsídeo/genética , Pré-Escolar , Comorbidade , Primers do DNA , Infecções por Enterobacteriaceae/epidemiologia , Fezes/virologia , Humanos , Lactente , Recém-Nascido , Rotavirus/genética , Rotavirus/isolamento & purificação , Estações do Ano , Sibéria/epidemiologia , População UrbanaRESUMO
A full-size human antibody to Ebola virus was constructed by joining genes encoding the constant domains of the heavy and light chains of human immunoglobulin with the corresponding DNA fragments encoding variable domains of the single-chain antibody 4D1 specific to Ebola virus, which was chosen from a combinatorial phage display library of single-strand human antibodies. Two expression plasmids. pCH1 and pCL1, containing the artificial genes encoding the light and heavy chains of human immunoglobulin, respectively, were constructed. Their cotransfection into the human embryonic kidney cell line HEK293T provided the production of a full-size recombinant human antibody. The affinity constant for the antibody was estimated by solid-phase enzyme-linked immunoassay to be 7.7 x 10(7) +/- 1.5 x 10(7) M(-1). Like the parent single-chain antibody 4DI, the resulting antibody bound the nucleoprotein of Ebola virus and did not interact with the proteins of Marburg virus.
Assuntos
Anticorpos Antivirais/biossíntese , Ebolavirus/imunologia , Proteínas Recombinantes/biossíntese , Anticorpos Antivirais/genética , Anticorpos Antivirais/imunologia , Linhagem Celular , Clonagem Molecular , Humanos , Nucleoproteínas/imunologia , Plasmídeos/genética , Proteínas Recombinantes/genética , Proteínas Recombinantes/imunologia , Transfecção , Proteínas do Core Viral/imunologiaRESUMO
Eight specific antibodies to live variola virus (VV), Ind-3a strain, and 7 antibodies to VV, Butler strain, were selected from the synthetic combinatorial phage display library on single-chain (scFv) human antibodies. Indirect solid-phase enzyme immunoassay showed the ability of these antibodies to bind the VV strains Ind-3a, Butler, Brazil-131, Kuw-5, and Congo-2. Moreover, earlier selected human scFv antibodies were also tested in the reaction of binding to the above VV strains. The experiments could reveal the antibodies that bound alastrim strains more effectively that did other VV strains. The nucleotide sequences encoding for the selected scFv antibodies were determined.
Assuntos
Anticorpos Antivirais/imunologia , Vírus da Varíola/imunologia , Sequência de Aminoácidos , Anticorpos Antivirais/biossíntese , Anticorpos Antivirais/genética , Técnicas de Química Combinatória , Reações Cruzadas , Humanos , Região Variável de Imunoglobulina/biossíntese , Região Variável de Imunoglobulina/genética , Região Variável de Imunoglobulina/imunologia , Biblioteca de Peptídeos , Proteínas Recombinantes/genética , Proteínas Recombinantes/imunologiaRESUMO
A library of human scFv antibodies displayed on the surface of bacteriophages (MRC, Cambridge, England) was panned against the Elstree strain of vaccinia virus (VACV), which resulted in the phage repertoire enriched with clones positive to the strain. Individual clones from the repertoire were screened for binding, independently, to the vaccinia and ectromelia viruses; phage antibodies to the orthopoxviruses were selected. Ten unique antibodies were identified after their Vh- and Vl-genes were sequenced. All selected antibodies were assayed by ELISA for binding to the vaccinia, cowpox and ectromelia viruses. Furthermore, all selected antibodies were assayed for binding with major alastrim strains of the live variola virus. According to the results, the above phage antibodies recognized genus-specific epitopes, some of which differed in their conformation.