<unk> <unk>  is a family of proteins present on the<unk>  surface of red blood cells (RBCs or<unk> s) that are infected by the malarial parasite<unk><unk> .<unk>  is synthesized during the parasite's blood stage <unk> c schizogony) inside the RBC, during which the clinical symptoms of<unk>  malaria are manifested. Acting as both an antigen and adhesion protein, it is thought to play a key role in the high level of virulence associated with P.<unk> . It was discovered in<unk> 984 when it was reported that infected RBCs had unusually large-sized cell<unk>  proteins, and these proteins had antibody-binding (antigenic) properties. An elusive protein, its chemical structure and molecular properties were revealed only after a decade, in<unk> 995. It is now established that there is not one but a large family of<unk>  proteins, genetically regulated (encoded) by a group of about 60 genes called var. Each P.<unk>  is able to switch on and off specific var genes to produce a functionally different protein, thereby evading the host's immune system. RBCs carrying<unk>  on their surface stick to endothelial cells, which facilitates further binding with uninfected RBCs (through the processes of sequestration and rosetting), ultimately helping the parasite to both spread to other RBCs as well as bringing about the fatal symptoms of P.<unk>  malaria.
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