scholarly journals Antibody Responses and Avidity of Naturally Acquired Anti-Plasmodium vivax Duffy Binding Protein (PvDBP) Antibodies in Individuals from an Area with Unstable Malaria Transmission

2011 ◽  
Vol 84 (6) ◽  
pp. 944-950 ◽  
Author(s):  
Sedigheh Zakeri ◽  
Akram Abouie Mehrizi ◽  
Navid Dinparast Djadid ◽  
Laleh Babaeekhou ◽  
Maryam Abbasi
2003 ◽  
Vol 71 (5) ◽  
pp. 2508-2515 ◽  
Author(s):  
Jia Xainli ◽  
Jennifer L. Cole-Tobian ◽  
Moses Baisor ◽  
Will Kastens ◽  
Moses Bockarie ◽  
...  

ABSTRACT Erythrocyte invasion by Plasmodium vivax is completely dependent on binding to the Duffy blood group antigen by the parasite Duffy binding protein (DBP). The receptor-binding domain of this protein lies within a cysteine-rich region referred to as region II (DBPII). To examine whether antibody responses to DBP correlate with age-acquired immunity to P. vivax, antibodies to recombinant DBP (rDBP) were measured in 551 individuals residing in a village endemic for P. vivax in Papua New Guinea, and linear epitopes mapped in the critical binding region of DBPII. Antibody levels to rDBPII increased with age. Four dominant linear epitopes were identified, and the number of linear epitopes recognized by semiimmune individuals increased with age, suggesting greater recognition with repeated infection. Some individuals had antibodies to rDBPII but not to the linear epitopes, indicating the presence of conformational epitopes. This occurred in younger individuals or subjects acutely infected for the first time with P. vivax, indicating that repeated infection is required for recognition of linear epitopes. All four dominant B-cell epitopes contained polymorphic residues, three of which showed variant-specific serologic responses in over 10% of subjects examined. In conclusion, these results demonstrate age-dependent and variant-specific antibody responses to DBPII and implicate this molecule in partial acquired immunity to P. vivax in populations in endemic areas.


2008 ◽  
Vol 67 (3) ◽  
pp. 270-278 ◽  
Author(s):  
I. P. Ceravolo ◽  
F. A. Souza-Silva ◽  
C. J. F. Fontes ◽  
E. M. Braga ◽  
A. P. Madureira ◽  
...  

2012 ◽  
Vol 17 (8) ◽  
pp. 989-1000 ◽  
Author(s):  
Flora S. Kano ◽  
Bruno A. M. Sanchez ◽  
Tais N. Sousa ◽  
Michaelis L. Tang ◽  
Jéssica Saliba ◽  
...  

Vaccine ◽  
2004 ◽  
Vol 22 (27-28) ◽  
pp. 3727-3737 ◽  
Author(s):  
Syed Shams Yazdani ◽  
Ahmad Rushdi Shakri ◽  
Paushali Mukherjee ◽  
Sanjeev Kumar Baniwal ◽  
Chetan E. Chitnis

2008 ◽  
Vol 377 (4) ◽  
pp. 1279-1283 ◽  
Author(s):  
Carolina Saravia ◽  
Paola Martinez ◽  
Diana S. Granados ◽  
Carolina Lopez ◽  
Claudia Reyes ◽  
...  

2007 ◽  
Vol 14 (6) ◽  
pp. 726-731 ◽  
Author(s):  
So-Hee Kim ◽  
Seung-Young Hwang ◽  
Yong-Seok Lee ◽  
In-Hak Choi ◽  
Sae-Gwang Park ◽  
...  

ABSTRACT Phage display of single-chain variable fragment (scFv) antibodies is a powerful tool for selecting important, useful, and specific human antibodies. We constructed a library from three patients infected with Plasmodium vivax. Panning on recombinant PvRII enriched a population of scFvs that recognized region II of the P. vivax Duffy binding protein (DBP). Three clones of scFvs that reacted with PvRII were selected, and their biological functions were analyzed. These scFvs inhibited erythrocyte binding to DBP. Clone SFDBII92 had the greatest affinity (dissociation constant = 3.62 × 10−8 M) and the greatest inhibition activity (50% inhibitory concentration ≈ 2.9 μg/ml) to DBP. Thus, we demonstrated that human neutralizing antibody could be made from malaria patients using phage display and that these neutralizing scFvs should prove valuable for developing both passive and active immunization strategies based on DBP.


2009 ◽  
Vol 78 (3) ◽  
pp. 1089-1095 ◽  
Author(s):  
Patchanee Chootong ◽  
Francis B. Ntumngia ◽  
Kelley M. VanBuskirk ◽  
Jia Xainli ◽  
Jennifer L. Cole-Tobian ◽  
...  

ABSTRACT Plasmodium vivax Duffy binding protein (DBP) is a merozoite microneme ligand vital for blood-stage infection, which makes it an important candidate vaccine for antibody-mediated immunity against vivax malaria. A differential screen with a linear peptide array compared the reactivities of noninhibitory and inhibitory high-titer human immune sera to identify target epitopes associated with protective immunity. Naturally acquired anti-DBP-specific serologic responses observed in the residents of a region of Papua New Guinea where P. vivax is highly endemic exhibited significant changes in DBP-specific titers over time. The anti-DBP functional inhibition for each serum ranged from complete inhibition to no inhibition even for high-titer responders to the DBP, indicating that epitope specificity is important. Inhibitory immune human antibodies identified specific B-cell linear epitopes on the DBP (SalI) ligand domain that showed significant correlations with inhibitory responses. Affinity-purified naturally acquired antibodies on these epitopes inhibited the DBP erythrocyte binding function greatly, confirming the protective value of specific epitopes. These results represent an important advance in our understanding of part of blood-stage immunity to P. vivax and some of the specific targets for vaccine-elicited antibody protection.


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