Faculty Opinions recommendation of Adaptation of the genetically tractable malaria pathogen Plasmodium knowlesi to continuous culture in human erythrocytes.

Author(s):  
Carlos Morel ◽  
Cristiana Santos de Macedo
2012 ◽  
Vol 110 (2) ◽  
pp. 531-536 ◽  
Author(s):  
R. W. Moon ◽  
J. Hall ◽  
F. Rangkuti ◽  
Y. S. Ho ◽  
N. Almond ◽  
...  

2018 ◽  
Vol 8 (1) ◽  
Author(s):  
Oliver Lyth ◽  
Gema Vizcay-Barrena ◽  
Katherine E. Wright ◽  
Silvia Haase ◽  
Franziska Mohring ◽  
...  

Parasitology ◽  
2016 ◽  
Vol 145 (1) ◽  
pp. 6-17 ◽  
Author(s):  
G. A. BUTCHER ◽  
G. H. MITCHELL

SUMMARYIn recent years, a malaria infection of humans in South East Asia, originally diagnosed as a known human-infecting species,Plasmodium malariae, has been identified as a simian parasite,Plasmodium knowlesi.This species had been subject to considerable investigation in monkeys since the 1930s. With the development of continuous culture of the erythrocytic stages of the human malarial parasite,Plasmodium falciparumin 1976, the emphasis in research shifted away from knowlesi. However, its importance as a human pathogen has provoked a renewed interest inP. knowlesi, not least because it too can be maintained in continuous culture and thus provides an experimental model. In fact, this parasite species has a long history in malaria research, and the purpose of this chapter is to outline approximately the first 50 years of this history.


PLoS ONE ◽  
2016 ◽  
Vol 11 (10) ◽  
pp. e0164272 ◽  
Author(s):  
Amuza Byaruhanga Lucky ◽  
Miako Sakaguchi ◽  
Yuko Katakai ◽  
Satoru Kawai ◽  
Kazuhide Yahata ◽  
...  

2018 ◽  
Vol 5 ◽  
Author(s):  
Manickam Yogavel ◽  
Jyoti Chhibber-Goel ◽  
Abhishek Jamwal ◽  
Swati Gupta ◽  
Amit Sharma

1988 ◽  
Vol 167 (6) ◽  
pp. 1873-1881 ◽  
Author(s):  
J D Haynes ◽  
J P Dalton ◽  
F W Klotz ◽  
M H McGinniss ◽  
T J Hadley ◽  
...  

A 135-kD parasite protein, a minor component of the Plasmodium knowlesi malaria radiolabeled proteins released into culture supernatant at the time of merozoite release and reinvasion, specifically bound to human erythrocytes that are invaded and carry a Duffy blood group determinant (Fya or Fyb), but did not bind to human erythrocytes that are not invaded and do not carry a Duffy determinant (FyFy). Specific anti-Duffy antibodies blocked the binding of the 135-kD protein to erythrocytes carrying that specific Duffy determinant. Purified 135-kD protein bound specifically to the 35-45-kD Duffy glycoprotein on a blot of electrophoretically separated membrane proteins from Fya and Fyb erythrocytes but not from FyFy erythrocytes. Binding of the 135-kD protein was consistently greater to Fyb than to Fya both on the blot and on intact erythrocytes. The 135-kD protein also bound to rhesus erythrocytes that are Fyb and are invaded, but not to rabbit or guinea pig erythrocytes that are Duffy-negative and are not invaded. Cleavage of the Duffy determinant by pretreating Fyb human erythrocytes with chymotrypsin greatly reduced both invasion and binding of the 135-kD protein, whereas pretreating Fyb erythrocytes with trypsin had little effect on the Duffy antigen, the 135-kD protein binding, or on invasion. However, instances of invasion of other enzyme-treated erythrocytes that are Duffy-negative and do not bind the 135-kD protein suggest that alternative pathways for invasion do exist.


2012 ◽  
Vol 11 (1) ◽  
pp. 228 ◽  
Author(s):  
Amma A Semenya ◽  
Tuan M Tran ◽  
Esmeralda VS Meyer ◽  
John W Barnwell ◽  
Mary R Galinski

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