The Pneumococcal Serine-Rich Repeat Protein Is an Intra-Species Bacterial Adhesin That Promotes Bacterial Aggregation In Vivo and in Biofilms
Figure 7
Recombinant BR interacts with pneumococci that carry amino acids 122–166 of PsrP.
A) The designated recombinant PsrP constructs were expressed and purified from E. coli. B) Micrographs of FITC-labeled bacteria following their incubation with CY3-labeled rBR or the designated truncated versions. Note that only Cy3-labeled rBR and rBR.A bound to TIGR4. Moreover, neither bound to T4 ΔpsrP. This suggests that recombinant BR binds to PsrP on the bacteria surface. C) Far Western blot examining the interaction of Gst-BR with cell lysates from E. coli expressing assorted rBR constructs spotted on a membrane. D) Co-immunoprecipitation of Gst-BR (65 kDa) from spiked E. coli lysates expressing His-tagged rBR constructs. E) Far Western blot examining the interaction of Gst-BR with purified rBR constructs and a synthesized peptide corresponding to AA 122–166. F) Far Western blot examining the interaction of a glycosylated PsrP construct purified from S. pneumoniae, PsrPSRR2(33)-HIS with glycosylated PsrP constructs expressed in TIGR4.