Abstract

The purpose of this proposal is to identify and characterize bacterial surface groups that react in a selective way with the Fc regions of a variety of different immunoglobulin classes and subclasses from various mammals. In particular, we propose to study the number of functionally distinct Fc receptors associated with group A streptococci. To date, two functionally distinct but antigenically related Fc receptors have been found associated with one group A streptococcal strain. Future studies will be directed toward fully characterizing these receptors. This will include studies of their physicochemical composition and cloning of the gene or genes coding for these proteins. In addition, the biological activities of these molecules for these Fc receptors will be studied. These studies will include measurement of the ability of Fc receptors to mediate complement activation in serum and measurement of their mitogenic potential for peripheral blood lymphocytes. The role of bacterial Fc receptors in the disease course and post-infection sequelae of certain infections will be explored as suitable reagents become available.

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Institute of Allergy and Infectious Diseases (NIAID)
Type
Research Project (R01)
Project #
5R01AI020445-05
Application #
3130130
Study Section
Bacteriology and Mycology Subcommittee 1 (BM)
Project Start
1983-08-01
Project End
1989-08-31
Budget Start
1987-08-01
Budget End
1988-08-31
Support Year
5
Fiscal Year
1987
Total Cost
Indirect Cost

  Institution

Name
University of Florida
Department
Type
Schools of Medicine
DUNS #
073130411
City
Gainesville
State
FL
Country
United States
Zip Code
32611

  Publications

Podbielski, A; Weber-Heynemann, J; Cleary, P P (1994) Immunoglobulin-binding FcrA and Enn proteins and M proteins of group A streptococci evolved independently from a common ancestral protein. Med Microbiol Immunol 183:33-42
Raeder, R; Boyle, M D (1993) Association of type II immunoglobulin G-binding protein expression and survival of group A streptococci in human blood. Infect Immun 61:3696-702
Raeder, R; Otten, R A; Chamberlin, L et al. (1992) Functional and serological analysis of type II immunoglobulin G-binding proteins expressed by pathogenic group A streptococci. J Clin Microbiol 30:3074-81
Otten, R A; Raeder, R; Heath, D G et al. (1992) Identification of two type IIa IgG-binding proteins expressed by a single group A streptococcus. J Immunol 148:3174-82
Otten, R A; Boyle, M D (1991) The mitogenic activity of type III bacterial Ig binding proteins (protein G) for human peripheral blood lymphocytes is not related to their ability to react with human serum albumin or IgG. J Immunol 146:2588-95
Raeder, R; Faulmann, E L; Boyle, M D (1991) Evidence for functional heterogeneity in IgG Fc-binding proteins associated with group A streptococci. J Immunol 146:1247-53
Coleman, S E; Brady, L J; Boyle, M D (1990) Colloidal gold immunolabeling of immunoglobulin-binding sites and beta antigen in group B streptococci. Infect Immun 58:332-40
Faulmann, E L; Otten, R A; Barrett, D J et al. (1989) Immunological applications of type III Fc binding proteins. Comparison of different sources of protein G. J Immunol Methods 123:269-81
Brady, L J; Boyle, M D (1989) Identification of non-immunoglobulin A-Fc-binding forms and low-molecular-weight secreted forms of the group B streptococcal beta antigen. Infect Immun 57:1573-81
Yarnall, M; Boyle, M D (1986) Identification of a unique receptor on a group A streptococcus for the Fc region of human IgG3. J Immunol 136:2670-3

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