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Infection and Immunity, March 2008, p. 1223-1229, Vol. 76, No. 3
0019-9567/08/$08.00+0     doi:10.1128/IAI.01356-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Physical Linkage of Naturally Complexed Bacterial Outer Membrane Proteins Enhances Immunogenicity{triangledown}

Henriette Macmillan, Junzo Norimine, Kelly A. Brayton, Guy H. Palmer, and Wendy C. Brown*

Department of Veterinary Microbiology and Pathology, Washington State University, Pullman, Washington 99164

Received 8 October 2007/ Returned for modification 26 November 2007/ Accepted 4 December 2007

The outer membrane proteins (OMPs) of bacterial pathogens are essential for their growth and survival and especially for attachment and invasion of host cells. Since the outer membrane is the interface between the bacterium and the host cell, outer membranes and individual OMPs are targeted for development of vaccines against many bacterial diseases. Whole outer membrane fractions often protect against disease, and this protection cannot be fully reproduced by using individual OMPs. Exactly how the interactions among individual OMPs influence immunity is not well understood. We hypothesized that one OMP rich in T-cell epitopes can act as a carrier for an associated OMP which is poor in T-cell epitopes to generate T-dependent antibody responses, similar to the hapten-carrier effect. Major surface protein 1a (MSP1a) and MSP1b1 occur as naturally complexed OMPs in the Anaplasma marginale outer membrane. Previous studies demonstrated that immunization with the native MSP1 heteromer induced strong immunoglobulin G (IgG) responses to both proteins, but only MSP1a stimulated strong CD4+ T-cell responses. Therefore, to test our hypothesis, constructs of CD4+ T-cell epitopes from MSP1a linked to MSP1b1 were compared with individually administered MSP1a and MSP1b1 for induction of MSP1b-specific IgG. By linking the T-cell epitopes from MSP1a to MSP1b1, significantly higher IgG titers against MSP1b1 were induced. Understanding how the naturally occurring intermolecular interactions between OMPs influence the immune response may lead to more effective vaccine design.

* Corresponding author. Mailing address: Department of Veterinary Microbiology and Pathology, Washington State University, Pullman, WA 99164-7040. Phone: (509) 335-6067. Fax: (509) 335-8529. E-mail: wbrown{at}vetmed.wsu.edu

{triangledown} Published ahead of print on 17 December 2007.

Editor: W. A. Petri, Jr.

Infection and Immunity, March 2008, p. 1223-1229, Vol. 76, No. 3
0019-9567/08/$08.00+0     doi:10.1128/IAI.01356-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Han, S., Norimine, J., Palmer, G. H., Mwangi, W., Lahmers, K. K., Brown, W. C. (2008). Rapid Deletion of Antigen-Specific CD4+ T Cells following Infection Represents a Strategy of Immune Evasion and Persistence for Anaplasma marginale. J. Immunol. 181: 7759-7769 [Abstract] [Full Text]  
  • Seo, G.-M., Cheng, C., Tomich, J., Ganta, R. R. (2008). Total, Membrane, and Immunogenic Proteomes of Macrophage- and Tick Cell-Derived Ehrlichia chaffeensis Evaluated by Liquid Chromatography-Tandem Mass Spectrometry and MALDI-TOF Methods. Infect. Immun. 76: 4823-4832 [Abstract] [Full Text]  
  • Noh, S. M., Brayton, K. A., Brown, W. C., Norimine, J., Munske, G. R., Davitt, C. M., Palmer, G. H. (2008). Composition of the Surface Proteome of Anaplasma marginale and Its Role in Protective Immunity Induced by Outer Membrane Immunization. Infect. Immun. 76: 2219-2226 [Abstract] [Full Text]  


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