نتایج جستجو برای: duffy binding protein

تعداد نتایج: 1447864  

2013
Sowmya Sampath Chris Carrico Joel Janes Sairam Gurumoorthy Claire Gibson Martin Melcher Chetan E. Chitnis Ruobing Wang William R. Schief Joseph D. Smith

Glycan masking is an emerging vaccine design strategy to focus antibody responses to specific epitopes, but it has mostly been evaluated on the already heavily glycosylated HIV gp120 envelope glycoprotein. Here this approach was used to investigate the binding interaction of Plasmodium vivax Duffy Binding Protein (PvDBP) and the Duffy Antigen Receptor for Chemokines (DARC) and to evaluate if gl...

2013
Terence J. Hadley II Zhao-hai Lu Kazimiera Wasniowska Alvin W. Martin Stephen C. Peiper Joseph Hesselgesser Richard Horuk

The human erythrocyte chemokine receptor has recently been shown to be identical to the Duffy blood group antigen and is expressed in multiple organs, including kidney. Here we have examined the molecular properties of the renal isoform. Immunoblot analysis of erythrocyte and kidney detergent lysates, with a monoclonal antibody (Fy6) to the Duffy antigen, revealed that the renal isoform had a m...

Journal: :The Journal of Experimental Medicine 1998
Qijun Chen Antonio Barragan Victor Fernandez Annika Sundström Martha Schlichtherle Anders Sahlén Johan Carlson Santanu Datta Mats Wahlgren

Severe Plasmodium falciparum malaria is characterized by excessive sequestration of infected and uninfected erythrocytes in the microvasculature of the affected organ. Rosetting, the adhesion of P. falciparum-infected erythrocytes to uninfected erythrocytes is a virulent parasite phenotype associated with the occurrence of severe malaria. Here we report on the identification by single-cell reve...

2016
Yang Cheng Feng Lu Bo Wang Jian Li Jin-Hee Han Daisuke Ito Deok-Hoon Kong Lubin Jiang Jian Wu Kwon-Soo Ha Eizo Takashima Jetsumon Sattabongkot Jun Cao Myat Htut Nyunt Myat Phone Kyaw Sanjay A. Desai Louis H. Miller Takafumi Tsuboi Eun-Taek Han

Plasmodium vivax, a major agent of malaria in both temperate and tropical climates, has been thought to be unable to infect humans lacking the Duffy (Fy) blood group antigen because this receptor is critical for erythrocyte invasion. Recent surveys in various endemic regions, however, have reported P. vivax infections in Duffy-negative individuals, suggesting that the parasite may utilize alter...

Journal: Vaccine Research 2014
Behrouz Vaziri, Navid D. Djadid, Sedigheh Mirkazemi, Sedigheh Zakeri, Vahideh Valizadeh,

  Background: The purity and correct folding of a recombinant protein is critical for any structural, biochemical and vaccine design studies. Plasmodium vivax Duffy binding protein-II is a leading vaccine candidate for vivax malaria. In the present study, the purification process of recombinant DBP-IX (a variant form of PvDBP-II) was optimized to achieve the highest yield and purity. Moreover, ...

Journal: :The Journal of infectious diseases 2002
Jennifer L Cole-Tobian Alfred Cortés Moses Baisor Will Kastens Jia Xainli Moses Bockarie John H Adams Christopher L King

The interaction between the Plasmodium vivax merozoite Duffy binding protein region II (DBPII) and the human erythrocyte Duffy antigen leads to infection. Highly polymorphic regions of this protein may have arisen as a mechanism to avoid host immunity. To examine whether immunity to P. vivax is directed against these polymorphic regions of DBPII, age-associated changes in the frequency of speci...

2014
Taís Nóbrega de Sousa Flora Satiko Kano Cristiana Ferreira Alves de Brito Luzia Helena Carvalho

Plasmodium vivax infects human erythrocytes through a major pathway that requires interaction between an apical parasite protein, the Duffy binding protein (PvDBP) and its receptor on reticulocytes, the Duffy antigen/receptor for chemokines (DARC). The importance of the interaction between PvDBP (region II, DBPII) and DARC to P. vivax infection has motivated our malaria research group at Oswald...

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