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Infection and Immunity, November 2008, p. 5373-5380, Vol. 76, No. 11
0019-9567/08/$08.00+0     doi:10.1128/IAI.01044-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Recruitment of Rab27a to Phagosomes Controls Microbial Antigen Cross-Presentation by Dendritic Cells{triangledown}

Seong Hyun Kim,1 Annelies Visser,1 Carin Cruijsen,1 Adrianus W. M. van der Velden,2,{dagger} and Marianne Boes1,3*

Department of Dermatology, Brigham and Women's Hospital and Harvard Medical School, 77 Avenue Louis Pasteur, Boston, Massachusetts 02115,1 Department of Microbiology and Molecular Genetics, Harvard Medical School, 200 Longwood Ave., Boston, Massachusetts 02115,2 Department of Pediatric Immunology, University Medical Center Utrecht, Wilhelmina Children's Hospital, Utrecht, The Netherlands3

Received 21 August 2008/ Returned for modification 22 August 2008/ Accepted 29 August 2008

Polyreactive immunoglobulins (Ig) and complement components are present in tissues and blood of healthy individuals. They facilitate pathogen uptake and inactivation in lysosomes of phagocytes and thereby provide rapid protection against infection. Dendritic cells (DCs) are phagocytes that can acquire peptides from phagocytosed antigen to elicit cytotoxic immune responses by CD8+ T lymphocytes. The mechanisms that select peptides for cross-presentation are not fully resolved. Here we investigated the role of polyreactive Ig and complement in directing phagosomal antigen processing for cross-presentation. Phagocytosis facilitated by serum opsonization required the presence of Ig for effective antigen cross-presentation of microbe-derived antigen. The presence of complement C3 in serum promoted phagocytosis, yet phagosomes were defective in antigen degradation. The small GTPase Rab27a was recently implicated in antigen cross-presentation and was rapidly recruited to phagosomes only when Ig was present. Our data suggest that prebinding of antigen by polyreactive Ig potentiates the efficiency of antigen cross-presentation to CD8+ T cells through recruitment of Rab27a.

* Corresponding author. Mailing address: Department of Dermatology, Brigham and Women's Hospital and Harvard Medical School, 77 Avenue Louis Pasteur, Boston, MA 02115. Phone: (617) 525-5569. Fax: (617) 525-5571. E-mail: mboes{at}umcutrecht.nl

{triangledown} Published ahead of print on 8 September 2008.

Editor: A. J. Bäumler

{dagger} Present address: Department of Molecular Genetics and Microbiology and Center for Infectious Diseases, Stony Brook University, State University of New York, Centers for Molecular Medicine, Room 240, Stony Brook, NY 11794-5120.

Infection and Immunity, November 2008, p. 5373-5380, Vol. 76, No. 11
0019-9567/08/$08.00+0     doi:10.1128/IAI.01044-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Yao, M., Liu, X., Li, D., Chen, T., Cai, Z., Cao, X. (2009). Late Endosome/Lysosome-Localized Rab7b Suppresses TLR9-Initiated Proinflammatory Cytokine and Type I IFN Production in Macrophages. J. Immunol. 183: 1751-1758 [Abstract] [Full Text]  


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