ABSTRACT
BACKGROUND AND OBJECTIVES: Biological false positive (BFP) reactivity by the Venereal Disease Research Laboratory (VDRL) test used for diagnosis of syphilis is a cause for concern. The use of the VDRL as a screening procedure is challenged by some studies. The aim of this study is to determine the prevalence of BFP reactions in different subject groups and to assess the usefulness of Treponema pallidum hemagglutination (TPHA) test in low titre VDRL reactive sera. MATERIALS AND METHODS: A total of 5785 sera from sexually transmitted diseases (STD) clinic attendees, antenatal clinic attendees, husbands of antenatal cases, peripheral health centres attendees (representing community population) and from patients referred from different OPDs/wards were screened for BFP reactions by the VDRL test. Sera reactive in the VDRL test were confirmed by the TPHA test. RESULTS: Out of 80 qualitative VDRL reactive sera, 68 had <1:8 titre on quantitation and TPHA was positive in 59 samples, indicating BFP reactivity in 0.2% in all the subject groups. BFP was nil in the community population. The male-to-female ratio of BFP reactions was 2:1. VDRL and TPHA positivity was highest (76%) in the age group of 20-29 years. The seroprevalence of syphilis varied from 0.4% to 3.5% in different patient groups. CONCLUSIONS: The results of this study highlight that the TPHA positivity was high (86.8%) in sera with VDRL titre less than 1:8. Therefore, for the diagnosis of syphilis, it is recommended that a confirmatory test such as TPHA should be performed on all sera with a reactive VDRL regardless of its titre.
ABSTRACT
Progastricsin (PGC) is a major seminal plasma protein having aspartyl proteinases-like activity and showing close sequence similarity to pepsins. PGC is also present as zymogen in gastric mucosa. In this article, we have reviewed all important features of PGC. Furthermore, we have compared all features of PGC with those of different aspartyl proteinases. The complete amino acid sequence of PGC reveals that it is composed of 374 residues (gastricsin moiety of 331 residues and the activation segment of 43 residues). The gene of human PGC is located at single locus on chromosome 6, whereas the human pepsinogen genetic locus is polymorphic and codes for at least three distinct polypeptide sequences on chromosome 11. The major useful function of PGC includes production of pro-antimicrobial substance in seminal plasma. The crystal structure of human PGC is known, which shows that it is quite similar to that of porcine pepsinogen. The tertiary structure of PGC is comprised of commonly bilobal structure with a large active-site cleft between the lobes. Two aspartate residues in the center of the cleft, namely Asp32 and Asp215, function as catalytic residues. The sequence and structural features of PGC indicate that it is diverged from its pepsinogen ancestor in the early phase of the evolution of gastric aspartyl proteinases. Our detailed review of PGC structure, function and activation mechanism will also be of interest to cancer biologists as well as gastroenterologists.
