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Immunochemical properties of the staphylococcal poly-N-acetylglucosamine surface polysaccharide.

Authors :
Maira-Litrán T
Kropec A
Abeygunawardana C
Joyce J
Mark G 3rd
Goldmann DA
Pier GB
Source :
Infection and immunity [Infect Immun] 2002 Aug; Vol. 70 (8), pp. 4433-40.
Publication Year :
2002

Abstract

Staphylococcus aureus and Staphylococcus epidermidis often elaborate adherent biofilms, which contain the capsular polysaccharide-adhesin (PS/A) that mediates the initial cell adherence to biomaterials. Biofilm cells produce another antigen, termed polysaccharide intercellular adhesin (PIA), which is composed of a approximately 28 kDa soluble linear beta(1-6)-linked N-acetylglucosamine. We developed a new method to purify PS/A from S. aureus MN8m, a strain hyperproducing PS/A. Using multiple analytical techniques, we determined that the chemical structure of PS/A is also beta(1-6)-N-acetylglucosamine (PNAG). We were unable to find N-succinylglucosamine residues in any of our preparations in contrast to previously reported findings (D. McKenney, K. Pouliot, Y. Wang, V. Murthy, M. Ulrich, G. Doring, J. C. Lee, D. A Goldmann, and G. B. Pier, Science 284:1523-1527, 1999). PNAG was produced with a wide range of molecular masses that could be divided into three major fractions with average molecular masses of 460 kDa (PNAG-I), 100 kDa (PNAG-II), and 21 kDa (PNAG-III). The purified antigens were not soluble at neutral pH unless first dissolved in 5 M HCl and then neutralized with 5 M NaOH. PNAG-I was very immunogenic in rabbits, but the responses of individual animals were variable. Immunization of mice with various doses (100, 50, or 10 microg) of PNAG-I, -II, and -III demonstrated that only PNAG-I was able to elicit an immunoglobulin G (IgG) immune response with the highest titers obtained with 100-microg dose. When we purified a small fraction of PNAG with a molecular mass of approximately 780 kDa (PNAG-780) from PNAG-I, significantly higher IgG titers than those in mice immunized with the same doses of PNAG-I were obtained, suggesting the importance of the molecular mass of PNAG in the antibody response. These results further clarify the chemical structure of PS/A and help to differentiate it from PIA on the basis of immunogenicity, molecular size, and solubility.

Details

Language :
English
ISSN :
0019-9567
Volume :
70
Issue :
8
Database :
MEDLINE
Journal :
Infection and immunity
Publication Type :
Academic Journal
Accession number :
12117954
Full Text :
https://doi.org/10.1128/IAI.70.8.4433-4440.2002