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. 2010 Dec 30;5(12):e15798. doi: 10.1371/journal.pone.0015798

Figure 6. Alteration of the aggregation domain mutants in Asc10 lowers the ability of E. faecalis to bind to valve tissue.

Figure 6

(A) Double aggregation domain mutant (OG1SSp [pCF10-5]) with N-terminal aggregation domain deletion and central aggregation 31-aa insertion. The mutant is unable to bind as well as Asc10+ OG1SSp (pCF10). (B) Single aggregation domain mutants bind as well as Asc10+ OG1SSp (pCF10) initially, but over time the gap between the Asc10+ OG1SSp (pCF10) and mutant grows increasingly. The data shown are a compilation of at least three experiments. * denotes p≤0.02, with respect to Asc10+ OG1SSp (pCF10) valve bacterial loads.