Journal: Infection and Immunity

Article Title: Human Platelets Recognize a Novel Surface Protein, PadA, on Streptococcus gordonii through a Unique Interaction Involving Fibrinogen Receptor GPIIbIIIa ▿ †

doi: 10.1128/IAI.00664-09

Figure Lengend Snippet: Phenotypic properties of S. gordonii mutants deficient in production of proteins encoded by padA, sspAB, or hsa. (A) SDS-PAGE of proteins extracted from the cell wall of S. gordonii and stained with silver nitrate; (B) corresponding Western blot reacted with polyclonal antibody to PadA fragment I (Fig. ​(Fig.1),1), which was specific for PadA; (C) corresponding Western blot reacted with polyclonal antibody to S. mutans antigen I/II (cross-reactive with SspA and SspB); (D) cell surface Hsa present on immobilized S. gordonii cells as detected by sWGA-biotin and horseradish peroxidase (HRP)-streptavidin. *, P < 0.0001. Lanes and bars: 1, wild-type DL1; 2, UB1890 padA::aad9; 3, UB1964 SGO_2004::aad9; 4, UB1968 SGO_2006::aad9; 5, UB1360 Δ(sspA sspB)::aad9; 6, UB1552 hsa::aphA3 Δ(sspAsspB)::aad9; 7, UB1545 hsa::aphA3; 8, UB2031 hsa::aphA3 padA::aad9. Positions of molecular mass protein markers are indicated in panels A and C. Error bars indicate SEM.

Article Snippet: Levels of binding of succinylated wheat germ agglutinin-biotin (sWGA) (EY Laboratories, San Mateo, CA) to immobilized streptococcal cells were used to assess cell surface expression of Hsa as described previously ( 15 ).

Techniques: SDS Page, Staining, Western Blot