NDLI: Antibody-enhanced pneumococcal adherence requires IgA1 protease.

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Antibody-enhanced pneumococcal adherence requires IgA1 protease.

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Antibody-enhanced pneumococcal adherence requires IgA1 protease.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Bae, Deborah Scamurra, Ronald W. Janoff, Edward N. Weiser, Jeffrey N. Ratner, Adam J. Fasching, Claudine
Description	Author Affiliation: Weiser JN ( Department of Microbiology, University of Pennsylvania School of Medicine, Philadelphia, PA 19104, USA. weiser@mail.med.upenn.edu);
Abstract	IgA, the major class of Ig in secretions, classically functions by interfering with microbial attachment to host tissues. Many mucosal pathogens, including Streptococcus pneumoniae, express an IgA1 protease that may circumvent the protective effects of this Ig subclass. Because these proteases are specific for human IgA1, we generated human mAbs to the major surface antigen of the pneumococcus, its capsular polysaccharide, and tested their effect in a colonization model of bacterial adherence to respiratory epithelial cells in culture. Rather than inhibiting adherence, type-specific IgA1 markedly enhanced bacterial attachment to host cells, but only when cleaved by IgA1 protease. Neither antibodies of protease-insensitive subclasses (IgA2 and IgG) nor those directed against heterologous capsules had such activity. The adherence-promoting properties of cleaved antibodies correlated with the cationic characteristics of their variable segments, suggesting that bound Fab fragments may neutralize the inhibitory effect of negatively charged capsules on adhesive interaction with host cells. Coating of pneumococci with anticapsular polysaccharide antibody unmasked the bacterial phosphorylcholine ligand, allowing for increased adherence mediated by binding to the platelet activating factor receptor on epithelial cells. In addition, our findings provide evidence for a novel function of bacterial IgA1 proteases. These enzymes may enable pathogens to subvert the antigen specificity of the humoral immune response to facilitate adhesive interactions and persistence on the mucosal surface.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	7
Volume Number	100
Language	English
Publisher	National Academy of Sciences
Publisher Date	2003-04-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Bacterial Adhesion Immunology Immunoglobulin A Immunoglobulin G Serine Endopeptidases Metabolism Streptococcus Pneumoniae Antibodies, Monoclonal Antibody Specificity B-Lymphocytes Cells, Cultured Respiratory Mucosa Microbiology Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S. Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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