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  • 1
    Online-Ressource
    Online-Ressource
    ANTI‐C‐CARBOHYDRATE ANTIBODIES AFTER PNEUMOCOCCAL VACCINATION
    Wiley ; 1982
    In:  Acta Pathologica Microbiologica Scandinavica Series C: Immunology Vol. 90C, No. 1-6 ( 1982-11), p. 353-355
    Details
    In: Acta Pathologica Microbiologica Scandinavica Series C: Immunology, Wiley, Vol. 90C, No. 1-6 ( 1982-11), p. 353-355
    Kurzfassung: Similar levels of naturally occurring anti‐pneumococcal C‐carbohydrate antibodies were found in 15 splenectomized children, 10 splenectomized adults and 12 healthy adult volunteers by enzymelinked immunosorbent assay. Vaccination with a 14‐valent pneumococcal capsular polysaccharide vaccine (Pneumovax©) that contains approximately 75 μg C‐carbohydrate per dose only led to small anti‐C‐carbohydrate antibody increases; they were significant, however, for all three groups (p 〈 0.05) but antibody fold increases were below 2 in 34 of the 37 individuals studied.
    Materialart: Online-Ressource
    ISSN: 0108-0202
    URL: Issue
    URL: Article
    DOI: 10.1111/apm.1982.90C.issue-1-6
    DOI: 10.1111/j.1699-0463.1982.tb01462.x
    RVK:
    XA 13160.C
    Sprache: Englisch
    Verlag: Wiley
    Publikationsdatum: 1982
    Standort Signatur Einschränkungen Verfügbarkeit
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  • 2
    Online-Ressource
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    Curvature of Synthetic and Natural Surfaces Is an Important Target Feature in Classical Pathway Complement Activation
    The American Association of Immunologists ; 2010
    In:  The Journal of Immunology Vol. 184, No. 4 ( 2010-02-15), p. 1931-1945
    Details
    In: The Journal of Immunology, The American Association of Immunologists, Vol. 184, No. 4 ( 2010-02-15), p. 1931-1945
    Kurzfassung: The binding of Abs to microbial surfaces followed by complement activation constitutes an important line of defense against infections. In this study, we have investigated the relationship between complement activation and the binding of human IgM Abs to surfaces with different curvatures. IgM Abs to dextran were shown to activate complement potently on dextran-coated particles having a diameter around 250 nm, whereas larger (600 nm) particles were less potent activators. This selectivity regarding particle dimension was also found for complement activation by colloidal substances of microbial origin. Peptidoglycan (PGN) is the major chemical component in the cell wall of Gram-positive bacteria. Fragments of purified PGN with sizes of ∼100 nm promoted complement activation effectively through the classical pathway. By contrast, larger or smaller fragments of PGN did not activate complement strongly. A careful analysis of PGN fragments released during planctonic growth of Staphylococcus aureus showed that these include curvatures that would permit strong IgM-mediated complement activation, whereas the curvature of intact cells would be less effective for such activation. Consistently, we found that the suspended PGN fragments were strong activators of complement through the classical pathway. We suggest that these fragments act as decoy targets for complement activation, providing protection for S. aureus against the host immune response to infection.
    Materialart: Online-Ressource
    ISSN: 0022-1767 , 1550-6606
    URL: Article
    DOI: 10.4049/jimmunol.0902214
    RVK:
    XA 54100
    RVK:
    XA 10000
    Sprache: Englisch
    Verlag: The American Association of Immunologists
    Publikationsdatum: 2010
    ZDB Id: 1475085-5
    Standort Signatur Einschränkungen Verfügbarkeit
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  • 3
    Online-Ressource
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    Relationship between Cell Surface Carbohydrates and Intrastrain Variation on Opsonophagocytosis of Streptococcus pneumoniae
    American Society for Microbiology ; 1999
    In:  Infection and Immunity Vol. 67, No. 5 ( 1999-05), p. 2327-2333
    Details
    In: Infection and Immunity, American Society for Microbiology, Vol. 67, No. 5 ( 1999-05), p. 2327-2333
    Kurzfassung: Streptococcus pneumoniae undergoes spontaneous phase variation between a transparent and an opaque colony phenotype, the latter being more virulent in a murine model of sepsis. Opaque pneumococci have previously been shown to express lower amounts of C polysaccharide (cell wall teichoic acid) and in this study were shown to have a higher content of capsular polysaccharide by immunoelectron microscopy. This report then examined the relationship between expression of these two cell surface carbohydrate structures and their relative contribution to the increased virulence of opaque variants. Comparison of genetically related strains showed that the differential content of capsular polysaccharide did not affect the amount of teichoic acid as measured by a capture enzyme-linked immunosorbent assay (ELISA). In contrast, when the teichoic acid structure was altered by replacing choline in the growth medium with structural analogs, the quantity of capsular polysaccharide as measured by a capture ELISA was decreased, demonstrating a linkage in the expression of the two surface carbohydrate structures. A standardized assay was used to assess the relative contribution of cell surface carbohydrates to opsonophagocytosis. The opaque variants required 1.2- to 30-fold more immune human serum to achieve 50% opsonophagocytic killing than did related transparent variants (types 6B and 9V). The opsonophagocytic titer was proportional to the quantity of capsular polysaccharide rather than teichoic acid. The major factor in binding of the opsonin, C-reactive protein (CRP), was also the amount of capsular polysaccharide rather than the teichoic acid ligand. Only for the transparent variant (type 6B), which bound more CRP, was there enhanced opsonophagocytic killing in the presence of this serum protein. Increased expression of capsular polysaccharide, therefore, appeared to be the major factor in the decreased opsonophagocytic killing of opaque pneumococci.
    Materialart: Online-Ressource
    ISSN: 0019-9567 , 1098-5522
    URL: Article
    DOI: 10.1128/IAI.67.5.2327-2333.1999
    RVK:
    XA 10000
    Sprache: Englisch
    Verlag: American Society for Microbiology
    Publikationsdatum: 1999
    ZDB Id: 1483247-1
    Standort Signatur Einschränkungen Verfügbarkeit
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  • 4
    Online-Ressource
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    Effect of Capsulation of Opportunistic Pathogenic Bacteria on Binding of the Pattern Recognition Molecules Mannan-Binding Lectin, L-Ficolin, and H-Ficolin
    American Society for Microbiology ; 2005
    In:  Infection and Immunity Vol. 73, No. 2 ( 2005-02), p. 1052-1060
    Details
    In: Infection and Immunity, American Society for Microbiology, Vol. 73, No. 2 ( 2005-02), p. 1052-1060
    Kurzfassung: Mannan-binding lectin (MBL), L-ficolin, and H-ficolin are pattern recognition molecules of the innate immune system. We investigated their ability to bind to different serotypes and noncapsulated variants of two gram-positive bacterial species, Streptococcus pneumoniae and Staphylococcus aureus . MBL did not bind to capsulated S. aureus or capsulated S. pneumoniae but did bind to a noncapsulated S. aureus variant (Wood). L-ficolin bound to some capsulated S. aureus serotypes (serotypes 1, 8, 9, 11, and 12) and capsulated S. pneumoniae serotypes (11A, 11D, and 11F) but not to noncapsulated strains. H-ficolin did not bind to any of the S. pneumoniae and S. aureus serotypes included in this study but did bind to one strain of Aerococcus viridans . The concentrations of the three proteins in 97 plasma samples were estimated. The median concentrations were 0.8 μg per ml for MBL, 3.3 μg per ml for L-ficolin, and 18.4 μg per ml for H-ficolin.
    Materialart: Online-Ressource
    ISSN: 0019-9567 , 1098-5522
    URL: Article
    DOI: 10.1128/IAI.73.2.1052-1060.2005
    RVK:
    XA 10000
    Sprache: Englisch
    Verlag: American Society for Microbiology
    Publikationsdatum: 2005
    ZDB Id: 1483247-1
    Standort Signatur Einschränkungen Verfügbarkeit
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  • 5
    Online-Ressource
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    Method for Quantitative Detection and Presumptive Identification of Group B Streptococci on Primary Plating
    American Society for Microbiology ; 2003
    In:  Journal of Clinical Microbiology Vol. 41, No. 4 ( 2003-04), p. 1399-1403
    Details
    In: Journal of Clinical Microbiology, American Society for Microbiology, Vol. 41, No. 4 ( 2003-04), p. 1399-1403
    Kurzfassung: Maternal prenatal screening for group B streptococci (GBS) followed by offering of intrapartum chemoprophylaxis to carriers is one of the strategies used to reduce the incidence of neonatal early-onset GBS infections. Culturing of vaginal and anorectal swab specimens in selective broth is the screening procedure recommended by the Centers for Disease Control and Prevention. This technique is sensitive; it does not, however, allow either evaluation of the degree of colonization or detection of cocolonization with several GBS clones. We have examined the carriage rate and population dynamics of GBS in a group of Danish women during pregnancy and 1 year after delivery using a new detection method. In the present paper we describe a mixed blood agar medium (MB agar) that identifies GBS in the primary cultures by detection of a double hemolysis pattern consisting of characteristic, large zones of partial hemolysis (“CAMP zones”) and of narrow zones of complete hemolysis. The MB agar was at least as sensitive as culturing in selective broth for detection of GBS in vaginal and anorectal swab specimens, and GBS strains could be identified directly on the primary plate due to the CAMP zones without the need for subculturing. The carriage rate of GBS in a group of Danish women was found to be more than 30%, a figure considerably higher than the rate that was reported previously.
    Materialart: Online-Ressource
    ISSN: 0095-1137 , 1098-660X
    URL: Article
    DOI: 10.1128/JCM.41.4.1399-1403.2003
    RVK:
    XA 10000
    Sprache: Englisch
    Verlag: American Society for Microbiology
    Publikationsdatum: 2003
    ZDB Id: 1498353-9
    SSG: 12
    Standort Signatur Einschränkungen Verfügbarkeit
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  • 6
    Online-Ressource
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    Abundant human anti-Galα3Gal antibodies display broad pathogen reactivity
    Springer Science and Business Media LLC ; 2020
    In:  Scientific Reports Vol. 10, No. 1 ( 2020-03-12)
    Details
    In: Scientific Reports, Springer Science and Business Media LLC, Vol. 10, No. 1 ( 2020-03-12)
    Kurzfassung: Antibodies of the IgG class to terminal Galα3Gal (IgG anti-αGal) is abundant in human plasma and are reported to bind most sepsis-causing Gram-negative bacteria. However, these seminal findings, made more than two decades ago, have not been reexamined. Our aim was to assess IgG anti-αGal´s pathogen reactivity. We affinity purified IgG anti-αGal from a therapeutic grade normal human IgG pool applying two rounds of positive selection with Galα3Gal-coupled beads and included removal of column matrix reactive antibodies. The purified antibodies were rigorously characterized in terms of specificity and purity in various solid-phase immunoassays. We used flow cytometry to study reactivity against 100 consecutive clinical isolates diagnosed as cause of sepsis in humans. We found that the purified IgG anti-αGal displays high specificity for Galα3Gal. Also, IgG anti-αGal at 5 mg/L bound 56 out of 100 pathogens with predilection for Gram-positive bacteria binding 39 out of 52 strains. We confirm that although IgG anti-αGal comprise a small fraction of the human antibody pool (~0.1%), these antibodies targets an impressively large part of pathogens causing invasive disease.
    Materialart: Online-Ressource
    ISSN: 2045-2322
    URL: Article
    DOI: 10.1038/s41598-020-61632-9
    Sprache: Englisch
    Verlag: Springer Science and Business Media LLC
    Publikationsdatum: 2020
    ZDB Id: 2615211-3
    Standort Signatur Einschränkungen Verfügbarkeit
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  • 7
    Online-Ressource
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    Complement activation by human IgG antibodies to galactose‐ α ‐1,3‐galactose
    Wiley ; 2020
    In:  Immunology Vol. 161, No. 1 ( 2020-09), p. 66-79
    Details
    In: Immunology, Wiley, Vol. 161, No. 1 ( 2020-09), p. 66-79
    Kurzfassung: Some human antibodies may paradoxically inhibit complement activation on bacteria and enhance pathogen survival in humans. This property was also claimed for IgG antibodies reacting with terminal galactose‐α‐1,3‐galactose (Gal α 3Gal; IgG anti‐ α Gal), a naturally occurring and abundant antibody in human plasma that targets numerous different pathogens. To reinvestigate these effects, we used IgG anti‐ α Gal affinity isolated from a pool of normal human IgG and human hypogammaglobulinaemia serum as a complement source. Flow cytometry was performed to examine antibody binding and complement deposition on pig erythrocytes, Escherichia coli O86 and Streptococcus pneumoniae serotype 9V. Specific nanobodies were used to block the effect of single complement factors and to delineate the complement pathways involved. IgG anti‐ α Gal was capable of activating the classical complement pathway on all the tested target cells. The degree of activation was exponentially related to the density of bound antibody on E .  coli O86 and pig erythrocytes, but more linearly on S. pneumoniae 9V. The alternative pathway of complement amplified complement deposition. Deposited C3 fragments covered the activating IgG anti‐ α Gal, obstructing its detection and highlighting this as a likely general caveat in studies of antibody density and complement deposition. The inherent capacity for complement activation by the purified carbohydrate reactive IgG anti‐ α Gal was similar to that of normal human IgG. We propose that the previously reported complement inhibition by IgG anti‐ α Gal relates to suboptimal assay configurations, in contrast to the complement activating property of the antibodies demonstrated in this paper.
    Materialart: Online-Ressource
    ISSN: 0019-2805 , 1365-2567
    URL: Issue
    URL: Article
    DOI: 10.1111/imm.v161.1
    DOI: 10.1111/imm.13229
    RVK:
    XA 10000
    Sprache: Englisch
    Verlag: Wiley
    Publikationsdatum: 2020
    ZDB Id: 2006481-0
    Standort Signatur Einschränkungen Verfügbarkeit
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  • 8
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    International External Quality Assurance for Laboratory Identification and Typing of Streptococcus agalactiae (Group B Streptococci)
    American Society for Microbiology ; 2011
    In:  Journal of Clinical Microbiology Vol. 49, No. 4 ( 2011-04), p. 1475-1482
    Details
    In: Journal of Clinical Microbiology, American Society for Microbiology, Vol. 49, No. 4 ( 2011-04), p. 1475-1482
    Kurzfassung: We report the results from the first international multicenter external quality assessment (EQA) studies for molecular and serological typing of group B streptococcus (GBS) strains as part of DEVANI ( De sign of a V accine a gainst N eonatal I nfections), a pan-European program. A questionnaire-based surveillance was undertaken among eight laboratories participating in DEVANI and six laboratories not participating in DEVANI from 13 countries in order to assess their current microbiological procedures for GBS screening, diagnosis, and typing. GBS strains from three EQA distributions were characterized using molecular and serological methods based on GBS capsular polysaccharide typing. Participants were asked to test the first distribution using their current serotyping and genotyping methods. The Strep-B-Latex agglutination method was the most widely used method, with a typeability value of 〉 90%. A multiplex PCR assay for GBS capsular gene typing was also used by 2 of 14 centers, which achieved a typeability value of 93%; this assay detected only 9 of 10 GBS capsular polysaccharide genes. From the second and third EQA studies, standardized protocols were prepared for serological and molecular typing of GBS strains based on the Strep-B-Latex agglutination method and a novel multiplex PCR assay that detected all 10 GBS capsular types (Ia to IX). These standardized protocols are being used by many European laboratories, and as the use of these methods increases, it is imperative to continuously improve and assess laboratory performance and offer training to any laboratories that have technical difficulties.
    Materialart: Online-Ressource
    ISSN: 0095-1137 , 1098-660X
    URL: Article
    DOI: 10.1128/JCM.02365-10
    RVK:
    XA 10000
    Sprache: Englisch
    Verlag: American Society for Microbiology
    Publikationsdatum: 2011
    ZDB Id: 1498353-9
    SSG: 12
    Standort Signatur Einschränkungen Verfügbarkeit
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  • 9
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    Emergence and Global Dissemination of Host-Specific Streptococcus agalactiae Clones
    American Society for Microbiology ; 2010
    In:  mBio Vol. 1, No. 3 ( 2010-08-31)
    Details
    In: mBio, American Society for Microbiology, Vol. 1, No. 3 ( 2010-08-31)
    Kurzfassung: Group B streptococci (GBS) ( Streptococcus agalactiae ) have long been recognized as important causes of mastitis in cattle. After 1960, GBS also became the most prevalent cause of invasive and often fatal infections in newborns. At the same time, GBS are carried by a substantial proportion of healthy individuals. The aims of this study were to elucidate the genetic mechanisms that lead to diversification of the GBS population and to examine the relationship between virulence and host preference of evolutionary lineages of GBS. Genetic analysis of GBS isolates from worldwide sources demonstrated epidemic clones adapted specifically to either the human or bovine host. Such clones seem to emerge from a genetically heterogeneous core population as a result of recombination affecting major segments of the genome. Emergence and global spread of certain clones explain, in part, the change in epidemiology of GBS disease and may have implications for prevention.
    Materialart: Online-Ressource
    ISSN: 2161-2129 , 2150-7511
    URL: Article
    DOI: 10.1128/mBio.00178-10
    Sprache: Englisch
    Verlag: American Society for Microbiology
    Publikationsdatum: 2010
    ZDB Id: 2557172-2
    Standort Signatur Einschränkungen Verfügbarkeit
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  • 10
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    Temperature limitation may explain the containment of the trophozoites in the cornea during Acanthamoeba castellanii keratitis
    Springer Science and Business Media LLC ; 2014
    In:  Parasitology Research Vol. 113, No. 12 ( 2014-12), p. 4349-4353
    Details
    In: Parasitology Research, Springer Science and Business Media LLC, Vol. 113, No. 12 ( 2014-12), p. 4349-4353
    Materialart: Online-Ressource
    ISSN: 0932-0113 , 1432-1955
    URL: Article
    DOI: 10.1007/s00436-014-4109-0
    RVK:
    WA 15000
    Sprache: Englisch
    Verlag: Springer Science and Business Media LLC
    Publikationsdatum: 2014
    ZDB Id: 1462976-8
    SSG: 12
    Standort Signatur Einschränkungen Verfügbarkeit
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