scholarly journals Natural Human Antibody Responses to Plasmodium vivax Apical Membrane Antigen 1 under Low Transmission and Unstable Malaria Conditions in Sri Lanka

2006 ◽  
Vol 74 (1) ◽  
pp. 798-801 ◽  
Author(s):  
Thilan Wickramarachchi ◽  
Prasad H. Premaratne ◽  
K. L. R. Lakshman Perera ◽  
Sumith Bandara ◽  
Clemens H. M. Kocken ◽  
...  

ABSTRACT Plasmodium vivax apical membrane antigen 1, an important malaria vaccine candidate, was immunogenic during natural malaria infections in Sri Lanka, where low transmission and unstable malaria conditions prevail. Antibody prevalence increased with exposure in areas where malaria was or was not endemic. A marked isotype switch to cytophilic (immunoglobulin G1 [IgG1]/IgG3) antibodies was evident with increasing exposure exclusively in residents from areas of endemicity.

Vaccine ◽  
2011 ◽  
Vol 29 (43) ◽  
pp. 7491-7504 ◽  
Author(s):  
Sajani Dias ◽  
Maheshika Somarathna ◽  
Aresha Manamperi ◽  
Ananias A. Escalante ◽  
Anusha M. Gunasekera ◽  
...  

2004 ◽  
Vol 72 (1) ◽  
pp. 154-158 ◽  
Author(s):  
G. H. Mitchell ◽  
A. W. Thomas ◽  
G. Margos ◽  
A. R. Dluzewski ◽  
L. H. Bannister

ABSTRACT Apical membrane antigen 1 (AMA-1) of Plasmodium merozoites is established as a candidate molecule for inclusion in a human malaria vaccine and is strongly conserved in the genus. We have investigated its function in merozoite invasion by incubating Plasmodium knowlesi merozoites with red cells in the presence of a previously described rat monoclonal antibody (MAb R31C2) raised against an invasion-inhibitory epitope of P. knowlesi AMA-1 and then fixing the material for ultrastructural analysis. We have found that the random, initial, long-range (12 nm) contact between merozoites and red cells occurs normally in the presence of the antibody, showing that AMA-1 plays no part in this stage of attachment. Instead, inhibited merozoites fail to reorientate, so they do not bring their apices to bear on the red cell surface and do not make close junctional apical contact. We conclude that AMA-1 may be directly responsible for reorientation or that the molecule may initiate the junctional contact, which is then presumably dependent on Duffy binding proteins for its completion.


PLoS ONE ◽  
2009 ◽  
Vol 4 (4) ◽  
pp. e5254 ◽  
Author(s):  
Michele D. Spring ◽  
James F. Cummings ◽  
Christian F. Ockenhouse ◽  
Sheetij Dutta ◽  
Randall Reidler ◽  
...  

2005 ◽  
Vol 73 (4) ◽  
pp. 2444-2451 ◽  
Author(s):  
Julie Healer ◽  
Tony Triglia ◽  
Anthony N. Hodder ◽  
Alan W. Gemmill ◽  
Alan F. Cowman

ABSTRACT Plasmodium falciparum apical membrane antigen 1 (AMA1) is a leading malaria vaccine candidate whose function has not been unequivocally defined. Partial complementation of function can be achieved by exchanging the AMA1 of P. falciparum (PfAMA1) with that of P. chabaudi (PcAMA1). In this study, parasites expressing chimeric AMA1 proteins were created to identify domains of PfAMA1 critical in erythrocyte invasion and which are important immune targets. We report that specific chimeric AMA1 proteins containing domains I to III from PfAMA1 and PcAMA1 were able to complement PfAMA1 function in erythrocyte invasion. We demonstrate that domain III does not contain dominant epitope targets of antibodies raised against Escherichia coli expressed and refolded PfAMA1 ectodomain. Furthermore, we generated a parasite line in which the N-terminal pro region of PfAMA1 does not undergo proteolytic cleavage and show that its removal is necessary for PfAMA1 function.


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