Major glycoproteins in carp CNS myelin: Homology to P0 protein with HNK-1/L2 carbohydrate epitope

1993 ◽  
Vol 23 (3) ◽  
pp. 239-248 ◽  
Author(s):  
Kohtaro Takei ◽  
Kunio Kitamura ◽  
Koji Banno ◽  
Keiichi Uyemura
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.


2002 ◽  
Vol 226 (1) ◽  
pp. 42-50 ◽  
Author(s):  
Miriam S. Domowicz ◽  
Melissa M. Mueller ◽  
Todd E. Novak ◽  
Lauren E. Schwartz ◽  
Nancy B. Schwartz

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 ◽  
...  

2002 ◽  
Vol 83 (6) ◽  
pp. 1380-1388 ◽  
Author(s):  
Maryline Simon-Haldi ◽  
Ned Mantei ◽  
Jens Franke ◽  
Hans Voshol ◽  
Melitta Schachner

1987 ◽  
Vol 87 (1) ◽  
pp. 121-132
Author(s):  
K. Toda ◽  
D. Francis ◽  
G. Gerisch

Binding of a monoclonal antibody, mAb293, to cell-surface glycoproteins of Polysphondylium pallidum is known to be blocked by L-fucose, and Fab of this antibody has been shown to inhibit intercellular adhesion of aggregation-competent cells. Mutants with delayed expression of the carbohydrate epitope, ep293, recognized by the antibody, have been shown to be retarded and altered in cell aggregation. The present study shows that ep293 is a modification of carbohydrate structure that is subject to regulation not only in mutant but also in wild-type cells; ep293 is expressed at an early stage of exponential growth in wild-type and only after 12 h of starvation in mutant PN6002. Proteins are already glycosylated before the epitope is expressed. The developmental regulation of pallidin, a lectin known to be an unglycosylated protein, was investigated in parallel with ep293 using a monoclonal antibody. Pallidin was expressed at about the same time as the carbohydrate epitope in cells of the wild-type as well as the mutant. These results indicate a regulatory signal to which various events are coupled. Induction of ep293 and expression of pallidin are two of these events, and mutants such as PN6002 are altered in the timing of the signal.


2012 ◽  
Vol 109 (13) ◽  
pp. 4768-4773 ◽  
Author(s):  
J. M. Brown ◽  
J. Xia ◽  
B. Zhuang ◽  
K.-S. Cho ◽  
C. J. Rogers ◽  
...  

Sign in / Sign up

Export Citation Format

Share Document