scholarly journals Mammalian cell penetration, siRNA transfection, and DNA transfection by supercharged proteins

2009 ◽  
Vol 106 (15) ◽  
pp. 6111-6116 ◽  
Author(s):  
B. R. McNaughton ◽  
J. J. Cronican ◽  
D. B. Thompson ◽  
D. R. Liu
Keyword(s):  
Mammalian Cell ◽  
Dna Transfection ◽  
Cell Penetration ◽  
Sirna Transfection ◽  
Supercharged Proteins

Targeting intracellular bacteria with an extended cationic amphiphilic polyproline helix

2015 ◽  
Vol 13 (21) ◽  
pp. 5930-5936 ◽  
Author(s):  
Manish Nepal ◽  
Shankar Thangamani ◽  
Mohamed N. Seleem ◽  
Jean Chmielewski
Keyword(s):  
Antibacterial Activity ◽  
Mammalian Cell ◽  
Mammalian Cells ◽  
Pathogenic Bacteria ◽  
Intracellular Bacteria ◽  
Cell Penetration

Eradicating pathogenic bacteria that reside within mammalian cells is currently quite difficult. Herein we describe an agent with the dual properties of efficient mammalian cell penetration and potent antibacterial activity. Significantly, these activities can be combined to target pathogenic bacteria within macrophages.

Three-Dimensional Structure of Rotavirus-Fab Complex

1990 ◽  
Vol 48 (1) ◽  
pp. 238-239
Author(s):  
B.V.V. Prasad ◽  
E. Marietta ◽  
J.W. Burns ◽  
M.K. Estes ◽  
W. Chiu
Keyword(s):  
Image Processing ◽  
Smooth Surface ◽  
Three Dimensional ◽  
Outer Shell ◽  
Dimensional Structure ◽  
Structural Studies ◽  
Cell Penetration ◽  
Electron Cryomicroscopy ◽  
Image Processing Techniques ◽  
Processing Techniques

Rotaviruses are spherical, double-shelled particles. They have been identified as a major cause of infantile gastroenteritis worldwide. In our earlier studies we determined the three-dimensional structures of double-and single-shelled simian rotavirus embedded in vitreous ice using electron cryomicroscopy and image processing techniques to a resolution of 40Å. A distinctive feature of the rotavirus structure is the presence of 132 large channels spanning across both the shells at all 5- and 6-coordinated positions of a T=13ℓ icosahedral lattice. The outer shell has 60 spikes emanating from its relatively smooth surface. The inner shell, in contrast, exhibits a bristly surface made of 260 morphological units at all local and strict 3-fold axes (Fig.l).The outer shell of rotavirus is made up of two proteins, VP4 and VP7. VP7, a glycoprotein and a neutralization antigen, is the major component. VP4 has been implicated in several important functions such as cell penetration, hemagglutination, neutralization and virulence. From our earlier studies we had proposed that the spikes correspond to VP4 and the rest of the surface is composed of VP7. Our recent structural studies, using the same techniques, with monoclonal antibodies specific to VP4 have established that surface spikes are made up of VP4.

Metabolic biotinylation of mammalian cell receptors for imaging

2006 ◽  
Author(s):  
Bakhos A. Tannous ◽  
Jan Grimm ◽  
Katherine Perry ◽  
Ralph Weissleder ◽  
Xandra O. Breakefield
Keyword(s):  
Mammalian Cell ◽  
Cell Receptors

The Influence of Glycosylation on the Catalytic and Fibrinolytic Properties of Pro-Urokinase

1992 ◽  
Vol 68 (05) ◽  
pp. 539-544 ◽  
Author(s):  
Catherine Lenich ◽  
Ralph Pannell ◽  
Jack Henkin ◽  
Victor Gurewich
Keyword(s):  
Escherichia Coli ◽  
Mammalian Cell ◽  
Human Gene ◽  
Culture Media ◽  
Mammalian Cell Culture ◽  
Glycosylation Site ◽  
Clot Lysis ◽  
Cell Culture Media ◽  
E Coli ◽  
The Uk

SummaryWe previously found that human pro-UK expressed in Escherichia coli is more active in fibrinolysis than recombinant human pro-UK obtained from mammalian cell culture media. To determine whether this difference is related to the lack of glycosylation of the E. coli product, we compared the activity of E. coli-derived pro-UK [(-)pro-UK] with that of a glycosylated pro-UK [(+)pro-UK] and of a mutant of pro-UK missing the glycosylation site at Asn-302 [(-) (302) pro-UK]. The latter two pro-UKs were obtained by expression of the human gene in a mammalian cell. The nonglycosylated pro-UKs were activated by plasmin more efficiently (≈2-fold) and were more active in clot lysis (1.5-fold) than the (+)pro-UK. Similarly, the nonglycosylated two-chain derivatives (UKs) were more active against plasminogen and were more rapidly inactivated by plasma inhibitors than the (+)UK.These findings indicate that glycosylation at Asn-302 influences the activity of pro-UK/UK and could be the major factor responsible for the enhanced activity of E. coli-derived pro-UK.

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