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Updated: Aug 10, 2026

Capsular Serotyping of Streptococcus pneumoniae by Latex Agglutination
Published on: September 25, 2014
Capsule does not block antibody binding to PspA, a surface virulence protein of Streptococcus pneumoniae
Calvin C Daniels1, Travis C Briles, Shaper Mirza
1Department of Microbiology, University of Alabama at Birmingham, BBRB, 1530 3rd Ave North, Birmingham, AL 35294, USA.
Abstract:
Of the proteins on the surface of Streptococcus pneumoniae, one of those best able to elicit protection against pneumococcal infection is pneumococcal surface protein A (PspA). Although this protein is attached to the membrane molecule, lipoteichoic acid, which is well beneath the capsule, PspA's ability to inhibit complement deposition and killing by apolactoferrin, suggests that it must have surface exposure. This study provides quantitative data showing that the capsular polysaccharide on types 2 and 3 pneumococci provides little or no masking ability of antibodies to bind PspA. Capsule was even observed to enhance, rather than inhibit the binding of two protective monoclonal antibodies to their epitopes on cell surface PspA. These results with antibodies to PspA are in contrast to binding by antibodies to the phosphocholine (PC) epitope of the lipoteichoic and teichoic acids. The binding of antibody to PC was largely, but not completely, blocked by capsular polysaccharide.
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