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  • 1
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    International journal of immunogenetics 13 (1986), S. 0 
    ISSN: 1744-313X
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: The classification of antigens into TD, TI-1 and TI-2 varieties raises the question of whether responses to these antigens are produced by distinct or identical subpopulations of B cells. In the present study we have examined the extent of intraclonal specificity variation in the progeny of PFC appearing after stimulation with two unrelated antigens. Mouse lymphoid cells were stimulated with pairs of TD and TI antigens, PFC were individually cultured and daughter PFC examined for their specificity. In all combinations used, PFC responding to TD antigen engendered, after 48 h of culture, a high frequency of PFC daughters expressing one or the other antibody specificity, notwithstanding the specificity of parental PFC. However, PFC responding to TI antigens seemed less subject to variation in specificity, and PFC daughters engendered after a 48 h culture period were, in the majority, of the parental specificity. These results are analysed in relation to different subpopulations of B cells.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Oxford, U.K. and Cambridge, USA : Blackwell Science Ltd
    Scandinavian journal of immunology 44 (1996), S. 0 
    ISSN: 1365-3083
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: The authors have investigated the presence of serum-derived immunoglobulin G (IgG) fragments in the human intestine at various ages, these fragments possibly representing another source of antibodies in addition to secretory IgA (SIgA). Fab fragments of the γ isotype were found to be the major molecular form of immunoglobulins in the meconium (median value: 3.7 mg/g of stools), as compared with Fabα (75 μg/g) and IgM (2.6 μg/g). These fragments provided by molecules of the maternal serum displayed a strong antibody activity to the tetanus toxoid and were also found in the stools of 1-week-old babies fed with formula milk. The release of serum antibodies into the digestive lumen occurs largely via hepatobiliary secretions, as suggested by the presence of IgG antitoxins in the bile of children operated on extrahepatic biliary atresia. In adults, the Fab antitoxins were also detected in most stool extracts. Affinity of these molecules was found to be similar to that of their serum counterpart with a Ka of 2.1×1010 M1 (median value). These mucosal antibody fragments, associated with the normal pathway of serum IgG catabolism, could provide additional immune defences against pathogens, and be of importance to supplement an immature or deficient secretory immune system.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Scandinavian journal of immunology 34 (1991), S. 0 
    ISSN: 1365-3083
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Reactivity of the secretory protein Fv with immunoglobulins (Ig) from various species of vertebrates was investigated. Binding was observed throughout all taxonomic classes: mammalian, avian, reptilian, amphibian and fish. Contrasting with tins wide spectrum, no significant binding was found with most mammalian ungulates, such as horse (Perissodactl), cow, sheep and goat (Artiodactyls), Nevertheless disruption of’the hydrogen bonds of Ig allowed these non-reactive molecules lo bind. Such a conserved reactivity dining evolution, and our previous data on the effect of the cleavage of the intra-chain disulphide bonds, suggest that protein Fv recognizes a discontinuous framework structure involving both the FRI and FR3 regions in the variable domain of the heavy chain of Ig.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Oxford, UK; Malden, USA : Blackwell Science Ltd
    Scandinavian journal of immunology 59 (2004), S. 0 
    ISSN: 1365-3083
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: In a previous study, it was shown that an intramuscular administration of amino acid PADRE-ELDKWA sequence induced a mucosal immune response to a conserved epitope of human immunodeficiency virus in mice. In the same model, here it is shown that this method can be used with a selected peptide from the M protein of group A streptococci. The PADRE-ASREAK sequence was injected in mice by the intramuscular route. Antibodies against M protein were detected in extracts of mucosal tissues and in serum. The repertoire isotypes of serum immunoglobulin G (IgG) and mucosal IgA and IgG antibodies varied, according to the dose of injected peptide. The highest mucosal IgA antibody response was obtained with 0.01 µg of antigen per injection, whereas the systemic IgG antibody response increased with 10 µg of antigen. Mucosal antibody production against streptococci was confirmed by immunofluorescence analysis. These results provide evidence that this novel approach of mucosal vaccination may be of advantage for bacterial systems and suggest a new field of investigation based on synthetic peptide analogues.
    Type of Medium: Electronic Resource
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  • 5
    ISSN: 1365-3083
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: To improve the mucosal antibody response against a short amino acid (aa) sequence (ELDKWA) of HIV gp41, we have investigated a construction including this peptide in-line with the Pan DR epitope (PADRE). ELDKWA is a conserved peptide playing a key role in the pathogenicity of HIV transmission. PADRE is a non-natural peptide with multipotential immunogenic properties. The results show striking differences between mucosal and systemic immune systems, with a preferential response of the mucosal organs. In contrast with most mucosal immunizations, the intracellular response persists for over two months after the last injection. This strongly suggests that further investigations of conserved key epitopes from various pathogens may lead to safe and chemically defined mucosal vaccines with synthetic peptides. These candidate vaccines with free peptides may be suitable for mass campaigns even in developing countries.
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Scandinavian journal of immunology 42 (1995), S. 0 
    ISSN: 1365-3083
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: The molecular status of Abs in the vaginal fluid is reconsidered as a basis for immunization strategies for women's vaccination against HIV. Analysis of separated immunogiobulins (Igs) shows a large proportion of uncleaved IgG, whereas the low amount of IgA includes SIgA, monomers and fragments. SIgM is at a very low level, while free SC molecules are abundant. In addition to the already documented local synthesis, vaginal IgG contains serum-derived tetanus antitoxins. The IgG could reach the lumen by diffusion, and/or be transported by an Fc receptor-associated mechanism as suggested by the subclass imbalance in favour of the IgGl isotype. Vaginal SIgA contains very low levels of antibodies to the cell-wall carbohydrates from a dental caries-associated streptococcus confirming the participation of the secretory immune system. In addition, the low percentage of IgA2 suggests that a proportion of vaginal SIgA can also derive from actively transported serum polymers. In agreement with our previous studies showing induction of vaginal tetanus antitoxins by intramuscular immunization, these results are in favour of classical parenteral vaccinations to induce protection of the human vagina.
    Type of Medium: Electronic Resource
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  • 7
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Science Ltd
    Scandinavian journal of immunology 53 (2001), S. 0 
    ISSN: 1365-3083
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: The induction of a mucosal immunity provides an additional principle of vaccination by preventing the entry of pathogens in the body. Albeit the fact that intensive research has been conducted on local vaccines, the major mucosal vaccine commercially available for human use remains the oral polio vaccine. We have previously demonstrated that parenteral vaccination in humans with tetanus toxoid (TT) results in a genital immunoglobulin (Ig)G antibody (Ab) response. Here, we show that injections of TT with no adjuvant induces an anti-TT response in the mucosal tissues of normal BALB/c mice. The response is multiregional, involves both IgG and IgA isotypes, and is long-lasting. Similarly, injections of haptens coupled to TT or to other diffusible proteins may induce mucosal Abs. These results led us to immunize normal BALB/c mice with a viral peptide coupled to TT by disulfide bridging. The hapten was a 17 amino acid peptide containing the ELDKWA sequence of human immunodeficiency virus (HIV)-1 gp41. A significant IgG and IgA Ab response to the immunizing peptide was induced in various mucosal tissues despite the presence of a suboptimal Ab response in the spleen. The results indicate that mucosal immunity to peptides that are candidates for human vaccinations may be achieved by parenteral adjuvant-free immunization with peptide coupled to TT.
    Type of Medium: Electronic Resource
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  • 8
    Electronic Resource
    Electronic Resource
    Oxford, U.K. and Cambridge, USA : Blackwell Publishers
    Scandinavian journal of immunology 45 (1997), S. 0 
    ISSN: 1365-3083
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Protein-Fv (pFv) is a human B superantigen which can bind the variable domain (VH) of the heavy chain of immunoglobulins (Igs) and enhance the effector functions of secretory antibodies in the gut lumen. This study describes a rat molecule related to pFv by a similar specificity to the human VH3 domain. Investigation of the content of different gut segments shows that the rat pFv is usually hidden by its binding to local Igs to form macromolecular complexes similar to the immune fortresses described in normal humans. Furthermore, the pFv level generally increases from the jejunum to the colon in parallel with the decreasing water dilution, and finally a discontinuous presence can occur along the digestive tract. Detection of this molecule in the fetus proves its non-microbial origin. Variations of the release of pFv, according to the breeding and to littermating, suggest the influence of external factors. This animal model allows the development of a study of the functions of pFv in vivo using a current laboratory species and has already provided evidence that the synthesis of this important molecule of the secretory immune system is regulated by environmental factors.
    Type of Medium: Electronic Resource
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  • 9
    Electronic Resource
    Electronic Resource
    Amsterdam : Elsevier
    Journal of Chromatography A 440 (1988), S. 119-130 
    ISSN: 0021-9673
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 10
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Scandinavian journal of immunology 40 (1994), S. 0 
    ISSN: 1365-3083
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Protein Ev, a human sialoprotein recently described in the stools of patients suffering from liver diseases, binds the variable domain of the heavy chains of immunoglobulins. We show here that preincubation of this protein with monoclonal human IgG1 and IgM activates the complement cascade by forming nonimmune complexes, as evidenced by haemolysis inhibition of antibody-coated sheep erythrocytes. As negative controls, no inhibition was observed after incubation either with immunoglobulins or with protein Fv alone, and with the protein Ev-depleted medium. Activation was due to the binding of immunoglobulins with protein Fv, as shown by inhibition of protein Fv-induced agglutination of the sensitized erythrocytes in the absence of complement. Activation of the classical pathway was demonstrated both by using a buman IgG4 or F(ab)2 fragments unable to activate C1q, and by Western blot analysis of the cleavage of C4 in human serum. These results confirm that protein Fv-binding mimicks antigen-antibody reactions, and suggest its involvement in hepatitis-associated vasculitis and in local lesions of some infiammatory gut diseases.
    Type of Medium: Electronic Resource
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