Risk association of BST2 gene variants with disease progression in HIV-1 infected Indian cohort.

Bone marrow stromal cell antigen 2 (BST2) is an interferon induced host restriction factor for HIV-1 that blocks the release of nascent virions from infected T cells. We aimed to characterize BST2 gene variants in HIV-1 positive individuals in Indian cohort and study the association of these variants with disease progression in long term non progressors (LTNPs) and progressors. Archived samples of 32 LTNPs, 17 progressors, and 78 controls were screened for BST2 gene polymorphisms using Sanger's sequencing method.

Understanding the nano-bio interactions using real-time surface plasmon resonance tool.

Our current understanding of the biophysicochemical interactions at nano-bio interfaces is still very limited. Surface plasmon resonance (SPR) is a powerful tool for understanding the real-time kinetics of protein binding on the surface of nanoparticles (NPs) but has been least exploited for this purpose. In this study, we demonstrated the interaction of negatively charged poly lactic-co-glycolic acid (PLGA) NPs and positively charged chitosan oligosaccharide (COS)-coated PLGA NPs with two model proteins, namely bovine serum albumin (BSA) and hen egg white lysozyme (LYZ), at the physiological pH of 7.

How the surface functionalized nanoparticles affect conformation and activity of proteins: Exploring through protein-nanoparticle interactions.

To understand the effect of counter ions (Na) on the secondary conformation and functionality of the lysozyme, we have studied the interaction of lysozyme with counterion associated iron oxide nanoparticles (IONPs). The investigation was carried out at pH 7.4 and 9.

Inhibin anti-peptide antibody macromolecule: An approach to improve fecundity in Clarias batrachus.

Inhibins are members of the transforming growth factor beta (TGFβ) superfamily known to regulate ovarian functions through stimulation of the hypothalamo-pituitary-gonadal axis. In the present study, we aimed to design a species-specific inhibin-α chimeric peptide (ICP) and evaluate the effect of immunoneutralization using anti-ICP antisera to enhance the reproductive performance in female Clarias batrachus. Injection of anti-ICP antisera caused a significant increase in the number of oocytes at a medium dose (200 μl) in comparison to high dose (400 μl) and control (normal rabbit serum).

Molecular characterization of inhibin-A: Structure and expression analysis in Clarias batrachus.

The inhibins are disulphide-linked heterodimeric glycoproteins that belong to the TGFβ superfamily. Inhibins have been well studied in mammals but the information about their structure and function is very limited in lower vertebrates. The aim of the present study was to characterize inhibin-A and to understand its receptor binding interaction, and to evaluate its biological function in Clarias batrachus.

Assessing safety and protein interactions of surface-modified iron oxide nanoparticles for potential use in biomedical areas.

We have investigated the electrostatic interaction between bare iron oxide nanoparticles (IONPs) or low molecular weight chitosan coated iron oxide nanoparticles (LMWC-IONPs) and hen egg white lysozyme (HEWL) at different pH values using protein-nanoparticle reverse charge parity model. Physicochemical characterization of both IONPs and LMWC-IONPs were carried out using DLS, TEM, FE-SEM, XRD, TGA, XPS and VSM analysis. DLS, TEM and FE-SEM results indicated that both IONPs were monodispersed, with size ranging from 8 to 20nm.

Discordant HIV DNA PCR results among infants diagnosed with HIV infection and initiated on ART: a case series.

This case series reports three infants diagnosed with HIV-1 infection using DNA polymerase chain reaction (PCR) testing. The three children were initiated on antiretroviral therapy (ART) at ten, four and six months of age. Their serological tests at 18 months of age were negative for HIV-1.

The rs10993994 in the proximal MSMB promoter region is a functional polymorphism in Asian Indian subjects.

Background: The microseminoprotein gene encoding prostate secretory protein of 94 amino acids (PSP94) harbours a potential risk allele (rs10993994) for prostate cancer (PCa) in its promoter region. However, studies on rs10993994 have been sparse in Asian Indians.

Methods: The present study recruited a sample population of 44 benign prostatic hyperplasia patients, 33 PCa patients and 60 healthy participants, of which, participants without other confounding risk factors for PCa were retained.

Development of an ELISA for sPSP94 and utility of the sPSP94/sPSA ratio as a diagnostic indicator to differentiate between benign prostatic hyperplasia and prostate cancer.

Background: The serum PSA (sPSA) test has low specificity for prostate cancer (PCa), since sPSA also rises in benign prostatic hyperplasia (BPH). Serum PSP94 (sPSP94), a major secreted prostate protein, is indicated as a PCa marker. The potential of sPSP94 and sPSA in conjunction with each other to improve specificity of diagnostic test for PCa needs to be evaluated.

Effect of FSH receptor-binding inhibitor-8 on FSH-mediated granulosa cell signaling and proliferation.

Follicle-stimulating hormone is important for mammalian reproduction. It acts through specific receptors located on the plasma membrane of granulosa cells in ovaries and Sertoli cells in testes. The binding of follicle-stimulating hormone to its receptor activates intracytoplasmic signaling pathways leading to steroidogenesis.

Prostate Secretory Protein of 94 amino acids (PSP94) binds to prostatic acid phosphatase (PAP) in human seminal plasma.

Prostate Secretory Protein of 94 amino acids (PSP94) is one of the major proteins present in the human seminal plasma. Though several functions have been predicted for this protein, its exact role either in sperm function or in prostate pathophysiology has not been clearly defined. Attempts to understand the mechanism of action of PSP94 has led to the search for its probable binding partners.

Growth inhibition mediated by PSP94 or CRISP-3 is prostate cancer cell line specific.

The prostate secretory protein of 94 amino acids (PSP94) has been shown to interact with cysteine-rich secretory protein 3 (CRISP-3) in human seminal plasma. Interestingly, PSP94 expression is reduced or lost in the majority of the prostate tumours, whereas CRISP-3 expression is upregulated in prostate cancer compared with normal prostate tissue. To obtain a better understanding of the individual roles these proteins have in prostate tumourigenesis and the functional relevance of their interaction, we ectopically expressed either PSP94 or CRISP-3 alone or PSP94 along with CRISP-3 in three prostate cell lines (PC3, WPE1-NB26 and LNCaP) and performed growth inhibition assays.

High-affinity binding of seminal plasma PSP94 to human immunoglobulin is through the Fab domain.

Prostate secretory protein of 94 amino acids (PSP94) is one of the major proteins present in human seminal plasma. We had earlier reported that PSP94 has the ability to bind to human IgG. The aims of the present study were to further delineate the PSP94-IgG interaction and to understand whether this could have any significance in sperm function.

Crystal structure of prostate secretory protein PSP94 shows an edge-to-edge association of two monomers to form a homodimer.

Several recent genome-wide association studies have linked the human MSMB gene, encoding prostate secretory protein of 94 residues (PSP94), with prostate cancer susceptibility. PSP94 is one of the most abundant proteins from prostatic secretions and a primary constituent of human semen. PSP94 suppresses tumor growth and metastasis, and its expression gradually decreases during progression of the prostate cancer.

Interaction of follicle-stimulating hormone (FSH) receptor binding inhibitor-8: a novel FSH-binding inhibitor, with FSH and its receptor.

Follicle-stimulating hormone (FSH) receptor binding inhibitor (FRBI-8) is a novel octapeptide purified from human ovarian follicular fluid. In vitro, it inhibits the binding of FSH to granulosa cells and in vivo, it induces atresia in developing follicles in rodents. This peptide, when administered to marmosets and bonnet monkeys, altered the circulating progesterone levels.

Crystallization and preliminary X-ray diffraction analysis of human seminal plasma protein PSP94.

The human seminal plasma protein PSP94 is a small protein of 94 residues that contains ten cysteines. Since its discovery about 25 years ago, several potential biological functions have been reported for this protein. Many PSP94 homologues have also been identified since then from various species, but no crystal structure has been determined to date.

Disulphide bond reduction and S-carboxamidomethylation of PSP94 affects its conformation but not the ability to bind immunoglobulin.

Prostate secretory protein of 94 amino acids (PSP94) is a small non-glycosylated, cysteine rich protein with a molecular mass of 10 kDa. It has also been referred to as beta-microseminoprotein (beta-MSP) and proteins homologous to it have been reported in a number of species. Comparison of the amino acid sequence of these proteins suggests that, it is a rapidly evolving protein.