Article

Two Plasmodium falciparum merozoite proteins binding to erythrocyte band 3 form a direct complex.

Division of Cell Biology, Caritas St. Elizabeth's Medical Center, Tufts University School of Medicine, Boston, MA, USA.
Biochemical and Biophysical Research Communications (impact factor: 2.48). 01/2006; 338(4):1690-5. DOI:10.1016/j.bbrc.2005.10.154 pp.1690-5
Source: PubMed

ABSTRACT Erythrocyte invasion by malaria parasites requires multiple protein interactions. Our earlier studies showed that erythrocyte band 3 is an invasion receptor binding Plasmodium falciparum merozoite surface protein 1 and 9 (MSP1, MSP9) existing as a co-ligand complex. In this study, we have used biochemical approaches to identify the binding sites within MSP1 and MSP9 involved in the co-ligand complex formation. A major MSP9-binding site is located within the 19kDa C-terminal domain of MSP1 (MSP1(19)). Two specific regions of MSP9 defined as Delta1a and Delta2 interacted with native MSP1(19). The 42 kDa domain of MSP1 (MSP1(42)) bearing MSP1(19) in the C-terminus bound directly to both MSP9/Delta1a and Delta2. Thus, the regions of MSP1 and MSP9 interacting with the erythrocyte band 3 receptor are also responsible for assembling the co-ligand complex. Our evidence suggests a ternary complex is formed between MSP1, MSP9, and band 3 during erythrocyte invasion by P. falciparum.

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    Article: Identification of Bartonella Trw host-specific receptor on erythrocytes.
    Hon Kuan Deng, Danielle Le Rhun, Evelyne Le Naour, Sarah Bonnet, Muriel Vayssier-Taussat
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    ABSTRACT: Each Bartonella species appears to be highly adapted to one or a limited number of reservoir hosts, in which it establishes long-lasting intraerythrocytic bacteremia as the hallmark of infection. Recently, we identified Trw as the bacterial system involved in recognition of erythrocytes according to their animal origin. The T4SS Trw is characterized by a multiprotein complex that spans the inner and outer bacterial membranes, and possesses a hypothetical pilus structure. TrwJ, I, H and trwL are present in variable copy numbers in different species and the multiple copies of trwL and trwJ in the Bartonella trw locus are considered to encode variant forms of surface-exposed pilus components. We therefore aimed to identify which of the candidate Trw pilus components were located on the bacterial surface and involved in adhesion to erythrocytes, together with their erythrocytic receptor. Using different technologies (electron microscopy, phage display, invasion inhibition assay, far western blot), we found that only TrwJ1 and TrwJ2 were expressed and localized at the cell surface of B. birtlesii and had the ability to bind to mouse erythrocytes, and that their receptor was band3, one of the major outer-membrane glycoproteins of erythrocytes, (anion exchanger). According to these results, we propose that the interaction between TrwJ1, TrwJ2 and band 3 leads to the critical host-specific adherence of Bartonella to its host cells, erythrocytes.
    PLoS ONE 01/2012; 7(7):e41447. · 4.09 Impact Factor
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Keywords

19kDa C-terminal domain
 
42 kDa domain
 
band 3
 
binding sites
 
biochemical approaches
 
co-ligand complex
 
co-ligand complex formation
 
Delta1a
 
Delta2 interacted
 
erythrocyte band 3
 
erythrocyte band 3 receptor
 
Erythrocyte invasion
 
invasion receptor binding Plasmodium falciparum merozoite surface protein 1
 
major MSP9-binding site
 
malaria parasites
 
MSP1
 
MSP9 interacting
 
MSP9/Delta1a
 
multiple protein interactions
 
specific regions
 

Michael M Kariuki