Isolation of Low-Molecuter-Weight Lead-Binding Protein from Human Erythrocytes

1977 ◽  
Vol 155 (2) ◽  
pp. 164-167 ◽  
Author(s):  
S. R. V. Raghavan ◽  
H. C. Gonick
1998 ◽  
Vol 36 (3) ◽  
pp. 234-239 ◽  
Author(s):  
Yaxiong XIE ◽  
Momoko CHIBA ◽  
Atsuko SHINOHARA ◽  
Hiromi WATANABE ◽  
Yutaka INABA

2014 ◽  
Vol 10 (12) ◽  
pp. e1004532 ◽  
Author(s):  
Sanjeev Kumar ◽  
Saima Aslam ◽  
Mohit Mazumder ◽  
Pradeep Dahiya ◽  
Aruna Murmu ◽  
...  

2009 ◽  
Vol 77 (6) ◽  
pp. 2427-2435 ◽  
Author(s):  
Wai-Hong Tham ◽  
Danny W. Wilson ◽  
Linda Reiling ◽  
Lin Chen ◽  
James G. Beeson ◽  
...  

ABSTRACT Plasmodium falciparum invasion into human erythrocytes relies on the interaction between multiple parasite ligands and their respective erythrocyte receptors. The sialic acid-independent invasion pathway is dependent on the expression of P. falciparum reticulocyte binding protein-like homologue 4 (PfRh4), as disruption of the gene abolishes the ability of parasites to switch to this pathway. We show that PfRh4 is present as an invasion ligand in culture supernatants as a 160-kDa proteolytic fragment. We confirm that PfRh4 binds to the surfaces of erythrocytes through recognition of an erythrocyte receptor that is neuraminidase resistant but trypsin and chymotrypsin sensitive. Serum antibodies from malaria-exposed individuals show reactivity against the binding domain of PfRh4. Purified immunoglobulin G raised in rabbits against the binding domain of PfRh4 blocked the binding of native PfRh4 to the surfaces of erythrocytes and inhibited erythrocyte invasion of parasites using sialic acid-independent invasion pathways and grown in neuraminidase-treated erythrocytes. Our results suggest PfRh4 is a potential vaccine candidate.


FEBS Letters ◽  
1990 ◽  
Vol 262 (1) ◽  
pp. 101-103 ◽  
Author(s):  
Donna J. Carty ◽  
Ravi Iyengar

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

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