Model of binding of RBC and WBC infected by P.<unk>  to endothelial cells. The primary function of<unk>  is to bind and attach RBCs to the wall of the blood vessels. The most important binding properties of P.<unk>  known to date are mediated by the head structure of<unk> , consisting of DBL domains and CIDRs. DBL domains can bind to a variety of cell receptors including thrombospondin (TSP), complement receptor 1 (CR1), chondroitin sulfate A (CSA), P-selectin, endothelial protein C receptor (EPCR), and heparan sulfate. The DBL domain adjacent to the head structure binds to ICAM-1. CIDRs mainly bind to a large variety of cluster determinant 36 (CD36). These bindings produce the pathogenic characteristics of the parasite, such as sequestration of infected cells in different tissues, invasion of RBCs, and clustering of infected cells by a process called rosetting. The RBC-binding site of<unk> . (A) The head structure (mauve = NTS region, grey = DBL1α1, orange = CIDR1γ) with the docked blood group A (green-blue-black sticks) and heparin (yellow-black sticks) molecules. (B) Detail of the RBC-binding site with bound molecules (yellow = C, blue =N, red = O). CIDR1 protein in the semi-conserved head structure is the principal and best understood adhesion site of<unk> . It binds with CD36 on endothelial cells. Only group B and C proteins are able to bind, and that too with only those having CIDRα2-6 sequence types. On the other hand, group A proteins have either CIDRα1 or CIDRβ/γ/δ, and they are responsible for the most severe condition of malaria. Binding with ICAM-1 is achieved through the DBLβ domain adjacent to the head structure. However, many<unk> s having DBLβ domain do not bind to ICAM-1, and it appears that only the DBLβ paired with C2 domain can to bind to ICAM-1. The DBLα-CIDRγ tandem pair is the main factor for rosetting, sticking together the infected RBC with the uninfected cells, and thereby clogging of the blood vessels. This activity is performed through binding with CR1. The most dangerous malarial infection is in the brain and is called cerebral malaria. In cerebral malaria, the<unk>  proteins involved are DC8 and DC13. They are named after the number of domain cassettes they contain, and are capable of binding not only endothelial cells of the brain, but also in different organs including brain, lung, heart, and bone marrow. Initially, it was assumed that<unk>  binds to ICAM-1 in the brain, but DC8 and DC13 were found incompatible with ICAM-1. Instead DC8 and DC13 specifically bind to EPCR using CIDRα sub-types such as CIDRα1.1, CIDRα1.4, CIDRα1.5 and CIDRα1.7. However, it was later shown that DC13 can bind to both ICAM-1 and EPCR. EPCR is thus a potential vaccine and drug target in cerebral malaria. VAR2CSA is unique in that it is mostly produced by the placenta during pregnancy (the condition called pregnancy-associated malaria, PAM, or placental malaria). The majority of PAM is therefore due to VAR2SCA. Unlike other<unk> , VAR2CSA binds to chondroitin sulfate A present on the vascular endothelium of the placenta. Although its individual domains can bind to CSA, its entire structure is used for complete binding. The major complication in PAM is low-birth-weight babies. However, women who survived the first infection generally develop an effective immune response. In P.<unk> -prevalent regions in Africa, pregnant women are found to contain high levels of antibody (immunoglobulin G, or IgG) against VAR2CSA, which protect them the placenta-attacking malarial parasite. They are noted for giving birth to heavier babies.
Plasmodium falciparum erythrocyte membrane protein 1
Adenovirus E1B protein
M protein 
Tumor-associated glycoprotein 72
Penicillin-binding proteins
T independent antigen 
Lipopolysaccharide binding protein
Tax gene product