Lance R. Thurlow

TL;DR: It is shown that both gelatinase (GelE) and serine protease (SprE) contribute to biofilm formation by E. faecalis and provide clues to how the activity of these proteases governs this developmental process, suggesting the interplay of two secreted and coregulated proteases is responsible for regulating autolysis and the release of high-molecular-weight eDNA.

TL;DR: Fratricide as the governing principle behind gelatinase (GelE)‐mediated cell death and eDNA release is described and a mechanism by which GelE and SprE may modify the cell wall affinity of proteolytically processed AtlA resulting in either a pro‐ or anti‐lytic outcome is addressed.

TL;DR: It is demonstrated that GelE can cleave the anaphylatoxin complement C5a and that this proteolysis leads to decreased neutrophil migration in vitro and in vivo, and suggested that of the two enterococcal proteases, gelatinase is the principal mediator of pathogenesis in endocarditis.

TL;DR: It is demonstrated that seven of the nine genes in the cps operon are essential for capsule production, indicating that serotypes A and B do not make a capsular polysaccharide, and the genetic basis for the difference in antigenicity between serotypes C and D is the presence of cpsF in serotype C strains.

TL;DR: It is demonstrated, using cultured macrophages, that capsule-producing E. faecalis strains of either serotype C or D are more resistant to complement-mediated opsonophagocytosis than unencapsulated strains and several mechanisms by which the presence of the capsule influences evasion of the innate immune response are provided.