RESUMO
The ability of influenza viruses from different hosts to bind to the intestinal epithelium of various birds (Anseriformes (Anatidae), Galliformes, Charadriiformes (sandpipers and sea gulls), Ciconiiformes (storks), Podicipediformes (grebes), and Gruiformes was studied. The composition of sialo-containing receptors on the epithelia was examined, by using lectins. Intestinal epitheliocytes of the Anatidae (Anseriformes) family was shown to have a low content of receptors binding both Sambucus nigra agglutinin (SNA) lectin specific to Siaalpha-6Gal, and Maackia amurensis agglutinin (MAA) lection specific to Siaalpha2-2Gal. Nevertheless, these cells well bound duck influenza viruses. The intestinal epithelium of Ciconiiformes, Podicipediformes, and Gruiformes well bound MMA lection, but avian influenza viruses weakly bound the latter. The intestinal cells of Gallinaceae bound both MMA and SNA lectins and avian and human influenza viruses. Thus, the composition of natural sialosides is different in various avian species whereas the receptor specificity of influenza viruses from various hosts reflects these differences. This can be accounted for by the differences in the ability of influenza viruses from different birds to break through the interspecies barrier, infecting mammals and human beings in particular.
Assuntos
Aves , Vírus da Influenza A/fisiologia , Influenza Aviária/virologia , Mucosa Intestinal/química , Mucosa Intestinal/metabolismo , Mucinas , Oligossacarídeos , Receptores Virais/química , Receptores Virais/metabolismo , Mucosa Respiratória/química , Mucosa Respiratória/metabolismo , Animais , Aves/classificação , Aves/virologia , Humanos , Lectinas , Macaca , Modelos Moleculares , Mucinas/análise , Oligossacarídeos/análise , Oligossacarídeos/metabolismo , Especificidade da EspécieRESUMO
The receptor properties of H1 and H2 influenza viruses (IV), isolated from duck, pig and man were studied by using the natural and synthetic sialoglycoconjugates. It was shown that viruses, isolated from different hosts, adapt themselves to the host cell receptors. The IV affinity was increasing to 6'sialy(N-acetyllactosamine) in proportion as amino acids (in positions 138, 190, 194 and 225), which are for avian IV, were increasingly replacing. Some of the porcine viruses display adaptation to the human receptor, i.e. 6'sialy(N-acetyllactosamine), however, all tested porcine influenza viruses, belonging to different evolution branches, acquired even more affinity to sulphated and fucozyled derivatives of 3'sialy(N-acetyliactosamine)-(Neu5AC alpha 2-3 g AL beta 1-4(fUC alpha 1-3)(6-sulfo)GlcNAc beta).
Assuntos
Evolução Biológica , Glicoproteínas de Hemaglutininação de Vírus da Influenza/fisiologia , Orthomyxoviridae/fisiologia , Receptores Virais/metabolismo , Adaptação Fisiológica , Aminoácidos/metabolismo , Amino Açúcares/química , Amino Açúcares/metabolismo , Animais , Patos , Glicoproteínas de Hemaglutininação de Vírus da Influenza/química , Glicoproteínas de Hemaglutininação de Vírus da Influenza/metabolismo , Humanos , Modelos Moleculares , Orthomyxoviridae/imunologia , Orthomyxoviridae/isolamento & purificação , Especificidade da Espécie , Sulfatos , SuínosRESUMO
The receptor properties of influenza virus (IF) isolates/SSSR/90/77 are studied. The isolates are peculiar for losing glycosylation sites (GS) at the Asn131 receptor-binding region (GS131) after passaging in mice and at the Asn158 region (GS158) after cultivation in the presence of mouse serum. The loss of each carbohydrate residue increases the influenza virus affinity for carbohydrate chains with the terminal group Neu5Ac alpha 2-6Gal and reduces its affinity for Neu5Ac alpha 2-3Gal receptors. The effect is more pronounced in the GS158-depleted virus. Upon substitution of asparagine by aspartic acid, the electrostatic component of virus binding to the receptor is altered because of the increased negative charge on hemagglutinin. The virus receptor phenotype changes depending on the cultivation conditions. The isolate adapted to mice has higher affinity to mouse lung cell receptors, while the virus propagated in chick embryos in the presence of inhibitors has higher affinity to allantoic membrane cells.
Assuntos
Vírus da Influenza A Subtipo H1N1 , Vírus da Influenza A/fisiologia , Receptores de Superfície Celular/metabolismo , Animais , Asparagina/metabolismo , Sítios de Ligação , Metabolismo dos Carboidratos , Membrana Celular/virologia , Embrião de Galinha/virologia , Glicosilação , Hemaglutininas/metabolismo , Vírus da Influenza A/patogenicidade , Pulmão/metabolismo , Pulmão/virologia , Camundongos , Mutação , Ácido N-Acetilneuramínico/metabolismo , Fenótipo , Eletricidade EstáticaRESUMO
There is growing evidence that the receptor-binding characteristics of influenza viruses are affected by the host-dependent glycosylation of viral hemagglutinin (HA). To better understand these effects, we propagated two variants of the human influenza virus USSR/90/77 (which differed by the mutation Asn131 reversible Asp131 in the glycosylation sequon of their HA) in either embryonated chicken eggs or MDCK cell. Those variants were then compared for their ability to bind soluble receptor analogs and to attach to receptors represented on a solid phase. The carbohydrate chain at position 131 of the HA (CHO 131) interfered with virus binding to soluble Sia2-6Gal-containing macromolecular receptors, but had little or no effect on its binding to Sia2-3Gal-containing macromolecules. This specificity could be explained by the different orientation of the asialic parts of the 2-3-linked sialosides versus 2-6-linked sialosides with respect to the receptor-binding site (Eisen et al., 1997, Virology 232, 19-31). In the case of virus attachment to solid-phase immobilized receptors, MDCK-grown viruses bound substantially more weakly than their egg-grown counterparts to receptors of avian origin, whereas binding to mammalian cell membranes was only marginally affected by differences in host-specific glycosylation of the virus. Our data indicated that the effects of the carbohydrate side chain of HA on virus receptor-binding activity are dependent on both the cells in which the virus was grown and the nature of the cellular receptors or intercellular inhibitors to which the virus binds.
Assuntos
Glicoproteínas de Hemaglutininação de Vírus da Influenza/metabolismo , Vírus da Influenza A Subtipo H1N1 , Vírus da Influenza A/metabolismo , Receptores Virais/metabolismo , Animais , Sítios de Ligação , Células Cultivadas/virologia , Galinhas , Cães , Glicosilação , Humanos , Vírus da Influenza A/fisiologia , Modelos Moleculares , Mutação , Óvulo , SolubilidadeRESUMO
A new approach to anti-influenza chemotherapy is based on the development of synthetic inhibitors of virus attachment to host cells. These inhibitors are prepared by anchoring the minimum receptor determinant of influenza virus, sialic acid, to polymeric or liposomal carriers. In this study, a series of poly(acrylic acid-co-acrylamides) and dextrans bearing pendant glycylamidobenzylsialoside groups were synthesized and evaluated for their binding to a panel of influenza A and B virus strains and for their ability to inhibit virus infectivity in cell culture. Significant type-, subtype-, and strain-specific variation in virus susceptibility to the synthetic inhibitors was observed. Among the viruses tested, H3 subtype strains evolved in humans since 1975 were the most sensitive, while the earlier H3 viruses and the type B strains were resistant. The virus-inhibitory potency of the polymeric sialosides correlated with their bindings to the virus, and was dependent on the virus affinity for the ligand, the density of the ligand, and the nature and molecular mass of the polymeric carrier. In embryonated eggs, the antiviral effect of poly(acryloyl-glycylamidobenzylsialoside-co-acrylic acid) was comparable to that of equine alpha 2-macroglobulin.
Assuntos
Antivirais/farmacologia , Vírus da Influenza A/fisiologia , Vírus da Influenza B/fisiologia , Sialoglicoproteínas/farmacologia , Replicação Viral/efeitos dos fármacos , Portadores de Fármacos , Vírus da Influenza A/efeitos dos fármacos , Vírus da Influenza B/efeitos dos fármacos , Polímeros/química , Receptores Virais/efeitos dos fármacos , Receptores Virais/metabolismo , Especificidade da Espécie , Relação Estrutura-Atividade , alfa-Macroglobulinas/farmacologiaRESUMO
Anomeric aminobenzylglycosides of Neu5Ac were coupled with the polyacrylate carrier and a number of synthetic polyvalent sialosides obtained were investigated as inhibitors of influenza virus attachment. The inhibitory activity of polymeric sialosides is highly dependent upon the Neu5Ac residue content and the nature of the carrier. The polyacrylic acid based polymer bearing 10 mol% of Neu5Ac is 3 orders of magnitude more potent inhibitor than the corresponding monovalent benzylsialoside and considerably more active than fetuin.
Assuntos
Antivirais/farmacologia , Orthomyxoviridae/metabolismo , Polímeros/farmacologia , Receptores Virais/antagonistas & inibidores , Ácidos Siálicos/farmacologia , Ligação Competitiva , Hemaglutininas/metabolismo , Peroxidase do Rábano Silvestre/metabolismo , Ácido N-Acetilneuramínico , Polímeros/análise , Polímeros/química , Receptores Virais/metabolismo , Ácidos Siálicos/análise , Ácidos Siálicos/química , Relação Estrutura-Atividade , alfa-Fetoproteínas/metabolismo , alfa-Fetoproteínas/farmacologiaRESUMO
55697 Ixodidae ticks of 35 species, belonging to 7 genera, were collected in Guinea in 1981-1983. Virological study of 29410 ticks was performed by intracerebral infection of newborn white mice. 49 viral strains were isolated. Authors identified 38 strains of the 8 following arboviruses: Dugbe, Bhanja, CGL-Congo (ecologically connected with ticks), blue tongue virus of sheep and Abadine (association with ticks was found for the first time), Kindia and Forekarya (the new viruses). Serological screening of cattle (by means of agar diffuse precipitation reaction) has demonstrated a wide distribution of isolated viruses in Guinea. Most active circulation was that of Abadine virus. Its peak was observed in the humid season, the period of Amblyomma variegatum imago domination on cattle, this tick being the main source and vector of the virus, as experimentally confirmed.
Assuntos
Arbovírus/isolamento & purificação , Carrapatos/microbiologia , África Ocidental , Animais , Anticorpos Antivirais/análise , Arbovírus/classificação , Arbovírus/imunologia , Bunyaviridae/classificação , Bunyaviridae/imunologia , Bunyaviridae/isolamento & purificação , Bovinos , Reoviridae/classificação , Reoviridae/imunologia , Reoviridae/isolamento & purificação , Estações do AnoRESUMO
In the process of the immunological approbation of several experimental batches of the triyalent subunit influenza vaccine Grippovac, the pronounced immunogenicity of the antigens of all strains contained in the vaccine was established; most of the vaccinees were found to retain sufficiently high antibody titers for a year, and the essential total increase of antibody titers was found to occur after a single booster immunization. The serological checking of the diagnosed cases of influenza among immunized and nonimmunized children, carried out in two boarding schools during the influenza epidemic in the winter of 1984-1985 provided the proofs of the high effectiveness of Grippovac in preventing viral influenza, types A and B: the decrease of influenza morbidity among the immunized children reached 79,5-67,2-66,5% and the total morbidity rate in influenza in these two boarding scholls dropped, on the average, 3,0-3,5 times.
Assuntos
Vírus da Influenza A/imunologia , Vírus da Influenza B/imunologia , Vacinas contra Influenza/imunologia , Vírion/imunologia , Adolescente , Adulto , Idoso , Anticorpos Antivirais/análise , Criança , Pré-Escolar , Avaliação de Medicamentos , Humanos , Imunização , Imunização Secundária , Lactente , Influenza Humana/prevenção & controle , Pessoa de Meia-Idade , Federação Russa , Fatores de TempoRESUMO
Experiments were carried out to clarify the effect of swelling coefficients of various samples of the polycondensation anion exchange resin FAF in the C1 form on its sorption properties. The anion exchange resin was used to eliminate contaminating proteins and low molecular weight agents from the allantois fluid and liver cultured cells of pigs. Thermal treatment of the anion exchange resin increased the coefficient of its swelling, leaving the structure unchanged. The resin structure was controlled by electron microscopy and X-ray scattering of low angle. When the resin samples with the swelling coefficients of 3.5 and 4.0 were used, 30-40% of proteins, 50% of reducing agents and neutral carbohydrates and a small quantity of phosphorus were adsorbed.