Effect of Anti-CD4 Antibody UB-421 on HIV-1 Rebound after Treatment Interruption.

Background: Administration of a single broadly neutralizing human immunodeficiency virus (HIV)-specific antibody to HIV-infected persons leads to the development of antibody-resistant virus in the absence of antiretroviral therapy (ART). It is possible that monotherapy with UB-421, an antibody that blocks the virus-binding site on human CD4+ T cells, could induce sustained virologic suppression without induction of resistance in HIV-infected persons after analytic treatment interruption.

Methods: We conducted a nonrandomized, open-label, phase 2 clinical study evaluating the safety, pharmacokinetics, and antiviral activity of UB-421 monotherapy in HIV-infected persons undergoing analytic treatment interruption.

UB-311, a novel UBITh amyloid β peptide vaccine for mild Alzheimer's disease.

Introduction: A novel amyloid β (Aβ) synthetic peptide vaccine (UB-311) has been evaluated in a first-in-human trial with patients of mild-to-moderate Alzheimer's disease. We describe translational research covering vaccine design, preclinical characterization, and phase-I clinical trial with supportive outcome that advances UB-311 into an ongoing phase-II trial.

Methods: UB-311 is constructed with two synthetic Aβ-targeting peptides (B-cell epitope), each linked to different helper T-cell peptide epitopes (UBITh) and formulated in a Th2-biased delivery system.

Ammonia photodissociation promoted by Si(100).

Using in situ X-ray photoelectron spectroscopy measurements after reaction, we show that hydrogen-terminated Si(100) perturbs the bonding of physisorbed NH3 enabling a photochemical decomposition pathway at wavelengths different from those characteristic of either the molecule in the gas phase or the semiconductor bandgap. UV illumination only of gas phase NH3 at partial pressures from 0.1 to 100 Torr produced a maximum at 10 Torr in the N surface coverage.

Site-specific UBITh amyloid-beta vaccine for immunotherapy of Alzheimer's disease.

The UBITh AD immunotherapeutic vaccine for Alzheimer's disease uses an amyloid-beta (Abeta) immunogen having two designer peptides that have been engineered to elicit anti-N terminal Abeta(1-14) antibodies while minimizing potential for the generation of adverse anti-Abeta immune responses. The vaccine has been further designed for minimization of inflammatory reactivities through the use of a proprietary vaccine delivery system that biases Th2 type regulatory T cell responses in preference to Th1 pro-inflammatory T cell responses. In vitro studies and in vivo studies in small animals, baboons and macaques show that anti-Abeta antibodies are generated with the expected N-terminus site-specificity, and that these antibodies have functional immunogenicities to neutralize the toxic activity of Abeta and promote clearance of plaque deposition.

Synthetic luteinizing hormone releasing hormone (LHRH) vaccine for effective androgen deprivation and its application to prostate cancer immunotherapy.

We have designed a peptide-based immunotherapeutic vaccine for treatment of androgen-responsive prostate cancer. The vaccine targets the luteinizing hormone-releasing hormone (LHRH) decapeptide that results in an androgen-deprivation immunotherapy. The design elements of the peptide immunogens are the LHRH peptide or B cell epitope synthetically linked to different promiscuous helper T cell (Th) sequences, the UBITh epitopes, derived from four natural pathogens for effective immunogenicity in outbred populations, and in some cases, also linked to an adjuvanting peptide from Yersinia invasin (Inv) protein.