scholarly journals A Suppressor Screen for AGO1 Degradation by the Viral F-Box P0 Protein Uncovers a Role for AGO DUF1785 in sRNA Duplex Unwinding

2018 ◽  
Vol 30 (6) ◽  
pp. 1353-1374 ◽  
Author(s):  
Benoît Derrien ◽  
Marion Clavel ◽  
Nicolas Baumberger ◽  
Taichiro Iki ◽  
Alexis Sarazin ◽  
...  
Keyword(s):  
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.


Genetics ◽  
1998 ◽  
Vol 149 (2) ◽  
pp. 833-841
Author(s):  
Yu Jiang ◽  
Al Scarpa ◽  
Li Zhang ◽  
Shelly Stone ◽  
Ed Feliciano ◽  
...  

Abstract The BET3 gene in the yeast Saccharomyces cerevisiae encodes a 22-kD hydrophilic protein that is required for vesicular transport between the ER and Golgi complex. To gain insight into the role of Bet3p, we screened for genes that suppress the growth defect of the temperature-sensitive bet3 mutant at 34°. This high copy suppressor screen resulted in the isolation of a new gene, called BET5. BET5 encodes an essential 18-kD hydrophilic protein that in high copy allows growth of the bet3-1 mutant, but not other ER accumulating mutants. This strong and specific suppression is consistent with the fact that Bet3p and Bet5p are members of the same complex. Using PCR mutagenesis, we generated a temperature-sensitive mutation in BET5 (bet5-1) that blocks the transport of carboxypeptidase Y to the vacuole and prevents secretion of the yeast pheromone α-factor at 37°. The precursor forms of these proteins that accumulate in this mutant are indicative of a block in membrane traffic between the ER and Golgi apparatus. High copy suppressors of the bet5-1 mutant include several genes whose products are required for ER-to-Golgi transport (BET1, SEC22, USO1 and DSS4) and the maintenance of the Golgi (ANP1). These findings support the hypothesis that Bet5p acts in conjunction with Bet3p to mediate a late stage in ER-to-Golgi transport. The identification of mammalian homologues of Bet3p and Bet5p implies that the Bet3p/Bet5p complex is highly conserved in evolution.


1994 ◽  
Vol 83 (2) ◽  
pp. 285-288 ◽  
Author(s):  
Pierluigi Baron ◽  
Michael Shy ◽  
John Kamholz ◽  
Guglielmo Scarlato ◽  
David Pleasure

2022 ◽  
Vol 8 ◽  
Author(s):  
Shimaa Abd El-Salam El-Sayed ◽  
Mohamed Abdo Rizk ◽  
Haitham Eldoumani ◽  
Shimaa Sobhy Sorour ◽  
Mohamad Alaa Terkawi ◽  
...  

The molecular identification and antigenic characterization of P0 protein in Babesia divergens, a blood parasite of veterinary and zoonotic importance, were carried out in this study for use in developing subunit vaccines against B. divergens infection. Recombinant protein encoding P0 (BdP0) was developed in Escherichia coli, and its antiserum was generated in mice for further molecular characterization. Anti-rBdP0 serum had a specific interaction with the corresponding legitimate B. divergens protein, as confirmed by Western blotting and indirect fluorescent antibody tests. ELISA was used to assess the immunogenicity of BdP0 in a group of 68 bovine field samples, and significant immunological reactivity was found in 19 and 20 positive samples of rBdp0 and B. divergens lysate, respectively. The in vitro growth of B. divergens cultures treated with anti-rBdP0 serum was significantly inhibited (p < 0.05). Furthermore, after 6 h of incubation with 2 mg/ml anti-rBdP0 serum, the ability of pre-incubated free merozoites to invade bovine erythrocytes was reduced by 59.88%. The obtained data suggest the possible use of rBdP0 as diagnostic antigen and may serve as a vaccine candidate against babesiosis caused by B. divergens either in animal or human.


FEBS Letters ◽  
1992 ◽  
Vol 307 (3) ◽  
pp. 361-366 ◽  
Author(s):  
Takahito Yazaki ◽  
Masayuki Miura ◽  
Hiroaki Asou ◽  
Kunio Kitamura ◽  
Shigeo Toya ◽  
...  

2018 ◽  
Vol 04 (02) ◽  
Author(s):  
Jacqueline C Alexander ◽  
Jihye Lee ◽  
August P Miguez ◽  
Jason E Webb ◽  
Te Wen Lo

2001 ◽  
Vol 188 (1-2) ◽  
pp. 43-49 ◽  
Author(s):  
Kazuyuki Ishida ◽  
Hiroaki Takeuchi ◽  
Ryosuke Takahashi ◽  
Kazunori Yoshimura ◽  
Masahito Yamada ◽  
...  

2007 ◽  
Vol 58 ◽  
pp. S227
Author(s):  
Takeshi Adachi ◽  
Masahiro Tomioka ◽  
Hirofumi Kunitomo ◽  
Yoshifumi Okochi ◽  
Ikue Mori ◽  
...  
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