scholarly journals Injectable tissue integrating networks from recombinant polypeptides with tunable order

2018 ◽  
Vol 17 (12) ◽  
pp. 1154-1163 ◽  
Author(s):  
Stefan Roberts ◽  
Tyler S. Harmon ◽  
Jeffrey L. Schaal ◽  
Vincent Miao ◽  
Kan (Jonathan) Li ◽  
...  
2008 ◽  
Vol 74 (23) ◽  
pp. 7431-7433 ◽  
Author(s):  
Mónica Martínez-Alonso ◽  
Nuria González-Montalbán ◽  
Elena García-Fruitós ◽  
Antonio Villaverde

ABSTRACT We have observed that a soluble recombinant green fluorescent protein produced in Escherichia coli occurs in a wide conformational spectrum. This results in differently fluorescent protein fractions in which morphologically diverse soluble aggregates abound. Therefore, the functional quality of soluble versions of aggregation-prone recombinant proteins is defined statistically rather than by the prevalence of a canonical native structure.


2000 ◽  
Vol 68 (7) ◽  
pp. 4312-4318 ◽  
Author(s):  
Sanchita Chatterjee ◽  
Subhash Singh ◽  
Rashmi Sohoni ◽  
Nevil J. Singh ◽  
Akhil Vaidya ◽  
...  

ABSTRACT Antibodies against the Plasmodium falciparum P0 ribosomal phosphoprotein (PfP0) have been detected exclusively but extensively in malaria-immune persons. Polyclonal rabbit and mice sera were raised against two recombinant polypeptides of P. falciparum P0 protein, PfP0N and PfP0C, covering amino acids 17 to 61 and the remaining amino acids 61 to 316, respectively. Sera against both these domains detected a 35-kDa protein fromPlasmodium yoelii subsp. yoelii, a rodent malarial parasite, and stained the surface of merozoites in immunofluorescence assays. Total immunoglobulin G (IgG) purified from rabbit and mouse anti-PfP0 sera by ammonium sulfate and DEAE-cellulose chromatography was used for passive transfer experiments in mice. Mice passively immunized with both anti-PfP0N and anti-PfP0C showed distinctly lower levels of parasitemia than control mice. With immunizations on days −1, 0, 1, 3, and 5, about 50% of both sets of mice receiving anti-PfP0N and anti-PfP0C cleared the lethal 17XL strain of P. yoelii and revived by day 25. All the control mice died by day 10. By extending the immunization schedule, the survival period of the mice could be extended for every mouse that received anti-PfP0 IgG. These data demonstrate the cross-protection of the anti-PfP0 IgG and establish parasite P0 protein as a target for invasion-blocking antibodies.


1989 ◽  
Vol 2 (6) ◽  
pp. 903
Author(s):  
G. Harcourt ◽  
Gillian Harcourt ◽  
D. Beeson ◽  
N. Willcox ◽  
A. Vincent ◽  
...  

1988 ◽  
Vol 10 (6) ◽  
pp. 607-617 ◽  
Author(s):  
ANTHONY A. HOLDER ◽  
ROBERT R. FREEMAN ◽  
STEPHEN C. NICHOLLS

2006 ◽  
Vol 189 (5) ◽  
pp. 1856-1865 ◽  
Author(s):  
Sami S. A. Ashgar ◽  
Neil J. Oldfield ◽  
Karl G. Wooldridge ◽  
Michael A. Jones ◽  
Greg J. Irving ◽  
...  

ABSTRACT Two putative autotransporter proteins, CapA and CapB, were identified in silico from the genome sequence of Campylobacter jejuni NCTC11168. The genes encoding each protein contain homopolymeric tracts, suggestive of phase variation mediated by a slipped-strand mispairing mechanism; in each case the gene sequence contained frameshifts at these positions. The C-terminal two-thirds of the two genes, as well as a portion of the predicted signal peptides, were identical; the remaining N-terminal portions were gene specific. Both genes were cloned and expressed; recombinant polypeptides were purified and used to raise rabbit polyclonal monospecific antisera. Using immunoblotting, expression of the ca.116-kDa CapA protein was demonstrated for in vitro-grown cells of strain NCTC11168, for 4 out of 11 recent human fecal isolates, and for 2 out of 8 sequence-typed strains examined. Expression of CapB was not detected for any of the strains tested. Surface localization of CapA was demonstrated by subcellular fractionation and immunogold electron microscopy. Export of CapA was inhibited by globomycin, reinforcing the bioinformatic prediction that the protein is a lipoprotein. A capA insertion mutant had a significantly reduced capacity for association with and invasion of Caco-2 cells and failed to colonize and persist in chickens, indicating that CapA plays a role in host association and colonization by Campylobacter. In view of this demonstrated role, we propose that CapA stands for Campylobacter adhesion protein A.


2018 ◽  
Vol 17 (12) ◽  
pp. 1164-1164
Author(s):  
Stefan Roberts ◽  
Tyler S. Harmon ◽  
Jeffrey L. Schaal ◽  
Vincent Miao ◽  
Kan (Jonathan) Li ◽  
...  

2018 ◽  
Vol 165 (4) ◽  
pp. 461-464 ◽  
Author(s):  
D. V. Grishin ◽  
D. D. Zhdanov ◽  
Yu. A. Gladilina ◽  
O. V. Podobed ◽  
V. S. Pokrovsky ◽  
...  

2020 ◽  
Vol 111 ◽  
pp. 110831
Author(s):  
Jingjing Xu ◽  
Yining Wang ◽  
Mengyao Ding ◽  
Guangzhou Song ◽  
Mingyang Wu ◽  
...  

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