High resolution X-ray structure of potent anti-HIV pokeweed antiviral protein-III

2003 ◽  
Vol 65 (10) ◽  
pp. 1709-1717 ◽  
Author(s):  
Igor V Kurinov ◽  
Fatih M Uckun
Keyword(s):  
High Resolution ◽  
Pokeweed Antiviral Protein ◽  
Antiviral Protein ◽  
X Ray ◽  
Anti Hiv

High Resolution X-Ray Structure and Potent Anti-HIV Activity of Recombinant Dianthin Antiviral Protein

2011 ◽  
Vol 54 (10) ◽  
pp. 692-702 ◽  
Author(s):  
Igor Kurinov ◽  
Francis Rajamohan ◽  
Fatih Uckun
Keyword(s):  
High Resolution ◽  
Antiviral Protein ◽  
X Ray ◽  
Anti Hiv

TXU (Anti-CD7)-Pokeweed Antiviral Protein as a Potent Inhibitor of Human Immunodeficiency Virus

1998 ◽  
Vol 42 (2) ◽  
pp. 383-388 ◽  
Author(s):  
Fatih M. Uckun ◽  
Lisa M. Chelstrom ◽  
Lisa Tuel-Ahlgren ◽  
Ilker Dibirdik ◽  
James D. Irvin ◽  
...  
Keyword(s):  
Human Immunodeficiency Virus ◽  
Scid Mouse ◽  
Pokeweed Antiviral Protein ◽  
Antiviral Protein ◽  
Cynomolgus Monkeys ◽  
Immunodeficiency Virus ◽  
Scid Mouse Model ◽  
Anti Hiv ◽  
Hiv 1

ABSTRACT We have evaluated the clinical potential of TXU (anti-CD7)-pokeweed antiviral protein (PAP) immunoconjugate (TXU-PAP) as a new biotherapeutic anti-human immunodeficiency virus (anti-HIV) agent by evaluating its anti-HIV type 1 (anti-HIV-1) activity in vitro, as well as in a surrogate human peripheral blood lymphocyte-severe combined immunodeficient (Hu-PBL-SCID) mouse model of human AIDS. The present report documents in a side-by-side comparison the superior in vitro anti-HIV-1 activity of TXU-PAP compared to the activities of zidovudine, 2′,3′-didehydro-2′,3′-dideoxythymidine, unconjugated PAP, and B53-PAP, an anti-CD4-PAP immunoconjugate. Notably, TXU-PAP elicited potent anti-HIV activity in the Hu-PBL-SCID mouse model of human AIDS without any side effects and at doses that were very well tolerated by cynomolgus monkeys. Furthermore, plasma samples from TXU-PAP-treated cynomolgus monkeys showed potent anti-HIV-1 activity in vitro.

scholarly journals Structure-Based Design and Engineering of a Nontoxic Recombinant Pokeweed Antiviral Protein with Potent Anti-Human Immunodeficiency Virus Activity

2003 ◽  
Vol 47 (3) ◽  
pp. 1052-1061 ◽  
Author(s):  
Fatih M. Uckun ◽  
Francis Rajamohan ◽  
Sharon Pendergrass ◽  
Zahide Ozer ◽  
Barbara Waurzyniak ◽  
...  
Keyword(s):  
Human Immunodeficiency Virus ◽  
Scid Mouse ◽  
Pokeweed Antiviral Protein ◽  
Antiviral Protein ◽  
Immunodeficiency Virus ◽  
Scid Mouse Model ◽  
Anti Hiv ◽  
Hiv 1

ABSTRACT A molecular model of pokeweed antiviral protein (PAP)-RNA interactions was used to rationally engineer FLP-102(151AA152) and FLP-105(191AA192) as nontoxic PAPs with potent anti-human immunodeficiency virus (anti-HIV) activities. FLP-102 and FLP-105 have been produced in Escherichia coli and tested both in vitro and in vivo. These proteins depurinate HIV type 1 (HIV-1) RNA much better than rRNA and are more potent anti-HIV agents than native PAP or recombinant wild-type PAP. They are substantially less toxic than native PAP in BALB/c mice and exhibit potent in vivo activities against genotypically and phenotypically nucleoside reverse transcriptase inhibitor-resistant HIV-1 in a surrogate human peripheral blood lymphocyte (Hu-PBL) SCID mouse model of human AIDS. Rationally engineered nontoxic recombinant PAPs such as FLP-102 and FLP-105 may provide the basis for effective salvage therapies for patients harboring highly drug-resistant strains of HIV-1. The documented in vitro potencies of FLP-102 and FLP-105, their in vivo antiretroviral activities in the HIV-infected Hu-PBL SCID mouse model, and their favorable toxicity profiles in BALB/c mice warrant the further development of these promising new biotherapeutic agents.

Electron microscopy of rabbit FC crystals

1983 ◽  
Vol 41 ◽  
pp. 730-731
Author(s):  
Robert A. Grant ◽  
Laura L. Degn ◽  
Wah Chiu ◽  
John Robinson
Keyword(s):  
Electron Microscopy ◽  
High Resolution ◽  
High Resolution Electron Microscopy ◽  
Molecular Replacement ◽  
X Ray ◽  
X Ray Crystallography ◽  
Resolution Electron ◽  
Replacement Technique ◽  
Hydrated Crystal ◽  
Molecular Structure Analysis

Proteolytic digestion of the immunoglobulin IgG with papain cleaves the molecule into an antigen binding fragment, Fab, and a compliment binding fragment, Fc. Structures of intact immunoglobulin, Fab and Fc from various sources have been solved by X-ray crystallography. Rabbit Fc can be crystallized as thin platelets suitable for high resolution electron microscopy. The structure of rabbit Fc can be expected to be similar to the known structure of human Fc, making it an ideal specimen for comparing the X-ray and electron crystallographic techniques and for the application of the molecular replacement technique to electron crystallography. Thin protein crystals embedded in ice diffract to high resolution. A low resolution image of a frozen, hydrated crystal can be expected to have a better contrast than a glucose embedded crystal due to the larger density difference between protein and ice compared to protein and glucose. For these reasons we are using an ice embedding technique to prepare the rabbit Fc crystals for molecular structure analysis by electron microscopy.

High Resolution Study of Polytypism: Application to SiC and Au3 Mn

1982 ◽  
Vol 40 ◽  
pp. 540-541
Author(s):  
G. Van Tendeloo ◽  
J. Van Landuyt ◽  
S. Amelinckx
Keyword(s):  
Electron Microscopy ◽  
High Resolution ◽  
Stacking Sequence ◽  
X Ray ◽  
Powerful Technique ◽  
Resolution Study ◽  
The Ideal

Polytypism has been studied for a number of years and a wide variety of stacking sequences has been detected and analysed. SiC is the prototype material in this respect; see e.g. Electron microscopy under high resolution conditions when combined with x-ray measurements is a very powerful technique to elucidate the correct stacking sequence or to study polytype transformations and deviations from the ideal stacking sequence.

A High Resolution Study of G.P. Zones in Aluminum - 4.2 at % Silver

1982 ◽  
Vol 40 ◽  
pp. 722-723 ◽  
Author(s):  
R. Gronsky
Keyword(s):  
Electron Microscopy ◽  
Transmission Electron Microscopy ◽  
High Resolution ◽  
Computer Simulations ◽  
Structural Characteristics ◽  
X Ray Diffraction ◽  
X Ray ◽  
Transmission Electron ◽  
Resolution Study

The phenomenon of clustering in Al-Ag alloys has been extensively studied since the early work of Guinierl, wherein the pre-precipitation state was characterized as an assembly of spherical, ordered, silver-rich G.P. zones. Subsequent x-ray and TEM investigations yielded results in general agreement with this model. However, serious discrepancies were later revealed by the detailed x-ray diffraction - based computer simulations of Gragg and Cohen, i.e., the silver-rich clusters were instead octahedral in shape and fully disordered, atleast below 170°C. The object of the present investigation is to examine directly the structural characteristics of G.P. zones in Al-Ag by high resolution transmission electron microscopy.

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