Inscrição na biblioteca: Guest
Portal Digital Begell Biblioteca digital da Begell eBooks Diários Referências e Anais Coleções de pesquisa
Critical Reviews™ in Immunology
Fator do impacto: 1.352 FI de cinco anos: 3.347 SJR: 1.022 SNIP: 0.55 CiteScore™: 2.19

ISSN Imprimir: 1040-8401
ISSN On-line: 2162-6472

Volumes:
Volume 39, 2019 Volume 38, 2018 Volume 37, 2017 Volume 36, 2016 Volume 35, 2015 Volume 34, 2014 Volume 33, 2013 Volume 32, 2012 Volume 31, 2011 Volume 30, 2010 Volume 29, 2009 Volume 28, 2008 Volume 27, 2007 Volume 26, 2006 Volume 25, 2005 Volume 24, 2004 Volume 23, 2003 Volume 22, 2002 Volume 21, 2001 Volume 20, 2000 Volume 19, 1999 Volume 18, 1998 Volume 17, 1997 Volume 16, 1996 Volume 15, 1995 Volume 14, 1994

Critical Reviews™ in Immunology

DOI: 10.1615/CritRevImmunol.v26.i4.40
pages 353-376

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

Kristian Riesbeck
Medical Microbiology, Department of Laboratory Medicine, Lund University, Malmö University Hospital, SE-205 02 Malmö, Sweden
Therese Nordstrom
Medical Microbiology, Department of Laboratory Medicine, Lund University, Malmö University Hospital, SE-205 02 Malmö, Sweden

RESUMO

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.


Articles with similar content:

Regulation of the Adhesion versus Cytotoxic Functions of the Mac-1/CR3/αMβ2 - lntegrin Glycoprotein
Critical Reviews™ in Immunology, Vol.20, 2000, issue 3
Gordon D. Ross
Regulation of the Formation and External Transport of Secretory Immunoglobulins
Critical Reviews™ in Immunology, Vol.19, 1999, issue 5-6
F.-E. Johansen, H. Schjerven, I. N. Norderhaug, P. Brandtzaeg
Expression and Function of Recombination Activating Genes in Mature В Cells
Critical Reviews™ in Immunology, Vol.18, 1998, issue 3
Masaki Hikida, Hitoshi Ohmori
Major Histocompatibility Complex (MHC) Class I Recognition by Natural Killer Cells
Critical Reviews™ in Immunology, Vol.17, 1997, issue 3-4
Marco Colonna, Christian Dohring
Toll Like Receptor-2 Signaling in Mycobacterium Tuberculosis Infection−A Double-Edged Sword
Forum on Immunopathological Diseases and Therapeutics, Vol.6, 2015, issue 3-4
Sadhna Sharma, Monika Sharma