Expanded Access to MGAWN1 in Subjects With: Suspected West Nile Neuroinvasive Disease; Suspected West Nile Virus Infection and a Compromised Immune System; or Substantial Accidental Exposure to West Nile Virus

This study will test an experimental drug called MGAWN1 for the treatment of West Nile infections.

Start Date-

Sponsor / Collaborator

MacroGenics, Inc.

[+1]

NCT00927953 / TerminatedPhase 2

Phase 2, Stratified, Randomized, Double-Blind, Placebo-Controlled Study to Evaluate Safety and Efficacy of MGAWN1 in Subjects With Laboratory-documented West Nile Fever or Suspected Central Nervous System Infection Due to West Nile Virus

This study will test a drug called MGAWN1 for the treatment of West Nile infections.

Start Date01 May 2009

Sponsor / Collaborator

MacroGenics, Inc.

[+1]

NCT00515385 / CompletedPhase 1

A Phase 1, Randomized, Double-Blind, Dose-Escalation Cohort Study to Evaluate the Safety, Tolerability and Pharmacokinetics of a Single Intravenous Infusion of MGAWN1, a Neutralizing, Humanized, Monoclonal Antibody (IgG1k) to West Nile Virus, in Healthy Adults

The primary purpose of this phase 1, double-blind, cohort study is to evaluate the safety, tolerability, and pharmacokinetics of escalating doses of MGAWN1 administered as a single intravenous (IV) infusion to healthy adults. Subjects will be enrolled sequentially into one of 5 dose-level cohorts, with 8 subjects in each cohort. Six subjects in each cohort will receive MGAWN1 (a Neutralizing, Humanized, Monoclonal Antibody (IgG1k) to West Nile Virus) and 2 will receive a saline control.

Start Date01 Aug 2007

Sponsor / Collaborator

MacroGenics, Inc.

[+1]

100 Clinical Results associated with WNV E protein

100 Translational Medicine associated with WNV E protein

0 Patents (Medical) associated with WNV E protein

Literatures (Medical) associated with WNV E protein

01 Sep 2023·Protein & Peptide Letters

Structural and Functional Analysis of Urease Accessory Protein E from Vancomycin-Resistance Staphylococcus aureus MU50 Strain

Article

Author: Ahmed, Aftab ; Choudhary, M Iqbal ; Atia-Tul-Wahab ; Siddiqui, Humaira

Background:An increasing prevalence of biofilm forming strains by vancomycinresistance Staphylococcus aureus (VRSA) is one of the most important causes of antimicrobial resistance. VRSA possesses various regulatory factors to form and sustain biofilm in biotic or abiotic conditions. Among them, ureolytic activity is an important factor in the stabilization of biofilms by neutralizing the acidic environment. Various urease accessory proteins are required to activate the urease enzyme inside the biofilm.Objective:To optimize the cloning, expression and purification of urease accessory protein E from VRSA for determination of the secondary structure, and functional characterization by using Berthelot’s method.Methods:BAB58453.1 gene (which encodes possible urease accessory protein E), having 38% similarity to Bacillus pasteurii UreE protein, was cloned, expressed, and purified by single-step affinity chromatography for performing secondary structural studies using circular dichroism spectroscopy, and functional analysis using Berthelot’s and crystal violet assay.Results:Structure elucidation using NMR and circular dichroism spectroscopy techniques revealed that UreE protein has a partially foldedα-helical structure. Using Berthelot's method, it was identified that the purified UreE protein has enhanced urease enzyme activity, in comparison to the control. From the results of Berthelot’s and crystal violet assays, it was deduced that the selected gene (UreE protein) plays a key role in enhancing urease enzyme activity and contributes to biofilm stability.Conclusion:Structural studies on VRSA urease accessory proteins could aid in the identification of new drug targets or the development of effective antibiofilm strategies (in combination with other drug targets) against infections caused by biofilm-producing strains.

01 Dec 2015·BMC Clinical Pathology

Expression of a-Tocopherol-Associated protein (TAP) is associated with clinical outcome in breast cancer patients

Article

Author: Beck, Rodney A ; Ring, Brian Z ; Yeh, Shuyuan ; Hicks, David G ; Seitz, Robert S ; Wang, Xi ; Ross, Douglas T ; Woolf, Kirsten

BACKGROUNDThe role of vitamin E in breast cancer prevention and treatment has been widely investigated, and the different tocopherols that comprise this nutrient have been shown to have divergent associations with cancer outcome. Our previous studies have shown that α-Tocopherol-associated protein (TAP), a vitamin E binding protein, may function as a tumor suppressor-like factor in breast carcinogenesis. The current study addresses the association of TAP expression with breast cancer clinical outcomes.METHODSImmunohistochemical stain for TAP was applied to a tissue microarray from a breast cancer cohort consisting of 271 patients with a median follow-up time of 5.2 years. The expression of TAP in tumor cells was compared with patient's clinical outcome at 5 years after diagnosis. The potential role of TAP in predicting outcome was also assessed in clinically relevant subsets of the cohort. In addition, we compared TAP expression and Oncotype DX scores in an independent breast cancer cohort consisting of 71 cases.RESULTSWe demonstrate that the expression of TAP was differentially expressed within the breast cancer cohort, and that ER+/PR ± tumors were more likely to exhibit TAP expression. TAP expression was associated with an overall lower recurrence rate and a better 5-year survival rate. This association was primarily in patients with ER+ tumors; exploratory analysis showed that this association was strongest in patients with node-positive tumors and was independent of stage and treatment with chemotherapy. TAP expression in ER/PR negative or triple negative tumors had no association with clinical outcome. In addition, we did not observe an association between TAP expression and Oncotype DX recurrence score.CONCLUSIONSThe significant positive association we found for α-Tocopherol-associated protein with outcome in breast cancer may help to better define and explain studies addressing α-tocopherol's association with cancer risk and outcome. Additionally, further studies to validate and extend these findings may allow TAP to serve as a breast-specific prognostic marker in breast cancer patients, especially in those patients with ER+ tumors.

01 Jun 2013·IUBMB LifeQ3 · BIOLOGY

Molecular phylogenetic analyses of albuminoids reveal the molecular evolution of allosteric properties

Q3 · BIOLOGY

Article

Author: Gabriella Fanali ; Alessandra di Masi ; Loris Leboffe ; Paolo Ascenzi ; Mauro Fasano ; Tiziana Alberio

AbstractSerum albumin, α‐fetoprotein, afamin (also named α‐albumin and vitamin E binding protein), and vitamin D binding protein are members of the albuminoid superfamily. Albuminoids are plasma proteins characterized by a marked ability for ligand binding and transport. Here, a focused phylogenetic analysis of sequence evolution by maximum likelihood of fatty acid binding sites FA1–FA7 of mammalian albuminoids reveals that the FA1, FA2, and FA3+FA4 sites in serum albumins have evolved from the most recent common ancestor through an intermediate that has originated the α‐fetoprotein and afamin clades. The same topology has been observed for the whole protein sequences, for the sequences of all the fatty acid binding sites (FA1–FA7) taken together, and for the allosteric core corresponding to residues 1–303 of human serum albumin. The quantitative divergence analysis indicates that the ligand binding cleft corresponding to the FA2 site could be the main determinant of allosteric properties of serum albumins only. In fact, this binding cleft is structurally not effective in vitamin D binding proteins, whereas key residues that serve to allocate the allosteric effectors are not present in afamins and α‐fetoproteins. © 2013 IUBMB Life, 65(6):544–549, 2013

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