These authors report that an increased load of G. vaginalis had both high negative and positive predictive values for the diagnosis of BV. While these molecular based diagnostic strategies are promising, the required expertise, laboratory resources and expense limits their use in the primary care setting. We demonstrate here that antibody-based techniques are an effective means of identifying G. vaginalis through the detection of its pore-forming toxin VLY. The ELISA based assay in particular, is sensitive. In addition to the diagnostic utility of these antibody-based strategies, they may have an additional role in the treatment of BV. We demonstrated antibody-mediated inhibition of lysis of erythrocytes as well as the likely target cell of GZD824 Dimesylate VLY in vivo, female genital tract epithelial cells. While successful eradication of BV in pregnant women is possible utilizing appropriate antimicrobial therapy, many women exhibit persistent symptoms, recurrent disease, and persistence of abnormal vaginal flora. Furthermore, several large clinical trials have demonstrated that the use of antibiotics in these women has not been associated with a reduction in preterm birth. The failure of antimicrobial therapy to reduce BV-associated preterm labor may be attributable its inability to mitigate the resultant inflammatory cascade already underway. The human-restricted activity of VLY represents a barrier to the study of pathogenesis and candidate therapeutic strategies. Disruption of the interaction of VLY with its host cell receptor, human CD59, may represent a novel approach to the treatment of BV. We demonstrated that polyclonal immune serum functions to inhibit the VLY-CD59 interaction, thereby reducing its toxic effects on a variety of human cell lines. These finding may serve as a preliminary basis for in vivo studies investigating a potential role for immunotherapy in the management of women with BV and the development of vaccine based strategies for Madrasin disease prevention. Proteases are enzymes which catalyze the hydrolysis of the peptide bonds in proteins. The selectivity for a specific amino acid sequence may be broad or narrow depending on the protease involved. Proteases are present in every extra- and intra-cellular compartment. Since uncontrolled proteolysis can be very deleterious for tissues, proteases are stored as inactive pro-enzymes that are activated only for specific and localized tasks limited in time. A tight control of the proteolytic activity is also performed by numerous endogenous protease inhibitors present at high concentration in all tissues or by compartmentalization like in the lysosomes. The Human Genome Project revealed more than 500 proteaseencoding genes. The substrate specificity, the trigger events and site of activation are still unknown for most of them. However, it is known that transient proteolysis is involved in many physiological situations like inflammation, coagulation, fibrinolysis, hormone generation, development or tissue turnover. Interestingly, persistent proteolysis has been observed in many diseases like cystic fibrosis, emphysema, rheumatoid arthritis, bacterial, viral and parasitic infections, tumor and metastasis spreading or pancreatitis. In the intracellular compartment apoptosis also involves specific proteolytic cascades. Thus many physiological and pathological events are closely related to persistent protease activity.