A Trichomonas vaginalis Rhomboid Protease and Its Substrate Modulate Parasite Attachment and Cytolysis of Host Cells
Fig 3
Serine protease activity and TvROM1 contribute to T. vaginalis attachment and lysis of ectocervical cells.
(A) Fluorescently labeled T. vaginalis incubated with ectocervical cell monolayers in the presence of increasing concentrations of the serine protease inhibitor 3,4-dichloroisocoumarin (3,4-DCI) followed by quantification of adhered parasites. The average fold change in attachment compared to vehicle control for four experiments each performed in triplicate is shown. Error bars denote the standard error, **p<0.01. (B) Parasites incubated with ectocervical cell monolayers in the presence of increasing 3,4-DCI followed by assessment of ectocervical cell lysis. The average fold change in cytolysis compared to vehicle control for three experiments performed in triplicate is shown. Error bars denote the standard error, **p<0.01. (C) Average fold difference in attachment of HA-TvROM1 transfectants compared to empty vector transfectants shown for four experiments each conducted in triplicate, with standard error shown as error bars, **p<0.01. (D) Average fold change in cytolysis of ectocervical cells by HA-TvROM1 transfectants compared to empty vector transfectants, results are from four experiments performed in triplicate. Standard error is shown as error bars, **p<0.01.