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Vaginal infections are a public health problem associated with serious health complications due to the exacerbated inflammation they generate. Vaginal inflammation may also occur in some noninfectious processes, such as noninfectious vaginitis and cytolytic vaginosis. Immune system cells respond to infections through various mechanisms, such as the formation of extracellular traps (ETs), which are DNA networks associated with effector proteins. Many pathogens induce ETs formation in vitro, as occurs in some natural infections. A recent report indicates that human vaginal infections in vivo generate ETs. Therefore, in this study, we aimed to identify ETs in samples from 40 donors who were diagnosed with infectious (i.e., bacterial vaginosis, candidiasis and trichomoniasis) and noninfectious (i.e., noninfectious vaginitis and cytolytic vaginosis) vaginal inflammation. We were able to observe ETs by identifying the LL‐37 peptide, which is associated with DNA networks. In seven vaginal swabs from the control group (formed by 19 donors without vaginal infection symptoms), we detected at least one pathogen per sample and observed ETs; thus, these donors were considered asymptomatic. The remaining 12 donors were confirmed to be healthy, as their exudates did not present any tested pathogens, sign of inflammation or ETs. ETs in vaginal inflammatory processes can worsen inflammation but may also help control infection. [ABSTRACT FROM AUTHOR]

The human parasite Entamoeba histolytica is an amitochondrial protozoan whose metabolism depends on glucose fermentation. Among the metabolic enzymes absolutely required for amoeba growth is the NAD+-dependent alcohol dehydrogenase (EhADH2). The polymeric form of EhADH2 was sedimented at 160,000 g, and in this fraction we observed [32P]-labeling of a 96-kDa protein under mono-ADP-ribosylation conditions with [32P]NAD+. The [32P]-labeled protein had the same molecular weight as the EhADH2 monomer. Because of the importance of monoADP-ribosylation in the regulation of many physiological processes, the aim of this study was to determine whether EhADH2 is ADP-ribosylated, and what would be the consequence of this modification on its alcohol and aldehyde dehydrogenase enzymatic activities. This study describes the ADP-ribosylation of EhADH2. This modification did not have an effect on the enzymatic activities, but it may regulate other functions of EhADH2. [ABSTRACT FROM AUTHOR]

Polyspecific antibodies bound to the cell surface of Entamoeba histolytica are polarized toward the uroid region and spontaneously released by the amoeba as supramolecular aggregate or cap. We purified these exfoliated structures and analyzed them by electron microscopy and sodium dodecyl sulfate electrophoresis. Isolated caps were mainly composed of membranes and contained five major [35S]methionine-Iabeled bands; many more bands appeared (together with immunoglobulins) after silver staining. Surface immunoprecipitates contained about twelve major [35S]methionine-Iabeled polypeptides, five of which had molecular weights similar to those of radiolabeled polypeptides in the cap. Some proteins in the caps had the same electrophoretic migration pattern as that from iodinated cell-surface proteins and polypeptides from isolated plasma membranes. Results suggest that only half of the surface-immunoprecipitated antigens are enriched in the cap. [ABSTRACT FROM PUBLISHER]