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.
journal_name
Infect Immunjournal_title
Infection and immunityauthors
Healer J,Triglia T,Hodder AN,Gemmill AW,Cowman AFdoi
10.1128/IAI.73.4.2444-2451.2005keywords:
subject
Has Abstractpub_date
2005-04-01 00:00:00pages
2444-51issue
4eissn
0019-9567issn
1098-5522pii
73/4/2444journal_volume
73pub_type
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journal_title:Infection and immunity
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journal_title:Infection and immunity
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journal_title:Infection and immunity
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journal_title:Infection and immunity
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doi:10.1128/IAI.6.4.616-627.1972
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journal_title:Infection and immunity
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journal_title:Infection and immunity
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journal_title:Infection and immunity
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更新日期:1999-07-01 00:00:00
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