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Critical Reviews™ in Immunology

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ISSN Druckformat: 1040-8401

ISSN Online: 2162-6472

The Impact Factor measures the average number of citations received in a particular year by papers published in the journal during the two preceding years. 2017 Journal Citation Reports (Clarivate Analytics, 2018) IF: 1.3 To calculate the five year Impact Factor, citations are counted in 2017 to the previous five years and divided by the source items published in the previous five years. 2017 Journal Citation Reports (Clarivate Analytics, 2018) 5-Year IF: 2.6 The Eigenfactor score, developed by Jevin West and Carl Bergstrom at the University of Washington, is a rating of the total importance of a scientific journal. Journals are rated according to the number of incoming citations, with citations from highly ranked journals weighted to make a larger contribution to the eigenfactor than those from poorly ranked journals. Eigenfactor: 0.00079 The Journal Citation Indicator (JCI) is a single measurement of the field-normalized citation impact of journals in the Web of Science Core Collection across disciplines. The key words here are that the metric is normalized and cross-disciplinary. JCI: 0.24 SJR: 0.429 SNIP: 0.287 CiteScore™:: 2.7 H-Index: 81

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Structure and Immunological Action of the Human Pathogen Moraxella catarrhalis IgD-Binding Protein

Volumen 26, Ausgabe 4, 2006, pp. 353-376
DOI: 10.1615/CritRevImmunol.v26.i4.40
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ABSTRAKT

Several pathogens have acquired the capacity to bind immunoglobulins in a nonimmune manner, that is, the binding does not involve the normal antigen-binding sites of the antibodies. In contrast to gram-positive bacteria, for example Staphylococus aureus, nonimmune binding to gram-negative bacteria is rare. Moraxella catarrhalis outer membrane protein MID is the first to date known IgD-binding protein. MID is a 200-kDa autotransporter protein that exists as an oligomer and is governed at the transcriptional level. The majority of M. catarrhalis clinical isolates expresses MID. Two functional domains have been attributed to MID. MID764-913 functions as an adhesin and promotes the bacteria to attach to epithelial cells. The IgD-binding domain is located within MID962-1200 and the IgD-binding is related to the secondary and tertiary structure, that is, an oligomer is required for an optimal interaction. In parallel, M. catarrhalis activates B lymphocytes through the IgD B-cell receptor. This stimulatory capacity can be blocked by anti-IgD polyclonal antibodies, and M. catarrhalis mutants devoid of MID do not stimulate B cells. Moreover, MID and MID962-1200 activates B lymphocytes in the presence of T-helper 2 cytokines or soluble CD40L. Thus, available data suggest that MID is a T-cell−independent antigen.

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