Biomaterial Database

Plasmodium falciparum malaria: band 3 as a possible receptor during invasion of human erythrocytes. 1985

V C Okoye, and V Bennett

Human erythrocyte band 3, a major membrane-spanning protein, was purified and incorporated into liposomes. These liposomes, at nanomolar concentrations of protein, inhibited invasion of human erythrocytes in vitro by the malaria parasite Plasmodium falciparum. Liposomes containing human band 3 were ten times more effective in inhibiting invasion than those with pig band 3 and six times more effective than liposomes containing human erythrocyte glycophorin. Liposomes alone or liposomes containing erythrocyte glycolipids did not inhibit invasion. These results suggest that band 3 participates in the invasion process in a step involving a specific, high-affinity interaction between band 3 and some component of the parasite.

UI	MeSH Term	Description	Entries
D008081	Liposomes	Artificial, single or multilaminar vesicles (made from lecithins or other lipids) that are used for the delivery of a variety of biological molecules or molecular complexes to cells, for example, drug delivery and gene transfer. They are also used to study membranes and membrane proteins.	Niosomes,Transferosomes,Ultradeformable Liposomes,Liposomes, Ultra-deformable,Liposome,Liposome, Ultra-deformable,Liposome, Ultradeformable,Liposomes, Ultra deformable,Liposomes, Ultradeformable,Niosome,Transferosome,Ultra-deformable Liposome,Ultra-deformable Liposomes,Ultradeformable Liposome
D008242	Lysogeny	The phenomenon by which a temperate phage incorporates itself into the DNA of a bacterial host, establishing a kind of symbiotic relation between PROPHAGE and bacterium which results in the perpetuation of the prophage in all the descendants of the bacterium. Upon induction (VIRUS ACTIVATION) by various agents, such as ultraviolet radiation, the phage is released, which then becomes virulent and lyses the bacterium.	Integration, Prophage,Prophage Integration,Integrations, Prophage,Prophage Integrations
D008288	Malaria	A protozoan disease caused in humans by four species of the PLASMODIUM genus: PLASMODIUM FALCIPARUM; PLASMODIUM VIVAX; PLASMODIUM OVALE; and PLASMODIUM MALARIAE; and transmitted by the bite of an infected female mosquito of the genus ANOPHELES. Malaria is endemic in parts of Asia, Africa, Central and South America, Oceania, and certain Caribbean islands. It is characterized by extreme exhaustion associated with paroxysms of high FEVER; SWEATING; shaking CHILLS; and ANEMIA. Malaria in ANIMALS is caused by other species of plasmodia.	Marsh Fever,Plasmodium Infections,Remittent Fever,Infections, Plasmodium,Paludism,Fever, Marsh,Fever, Remittent,Infection, Plasmodium,Plasmodium Infection
D008565	Membrane Proteins	Proteins which are found in membranes including cellular and intracellular membranes. They consist of two types, peripheral and integral proteins. They include most membrane-associated enzymes, antigenic proteins, transport proteins, and drug, hormone, and lectin receptors.	Cell Membrane Protein,Cell Membrane Proteins,Cell Surface Protein,Cell Surface Proteins,Integral Membrane Proteins,Membrane-Associated Protein,Surface Protein,Surface Proteins,Integral Membrane Protein,Membrane Protein,Membrane-Associated Proteins,Membrane Associated Protein,Membrane Associated Proteins,Membrane Protein, Cell,Membrane Protein, Integral,Membrane Proteins, Integral,Protein, Cell Membrane,Protein, Cell Surface,Protein, Integral Membrane,Protein, Membrane,Protein, Membrane-Associated,Protein, Surface,Proteins, Cell Membrane,Proteins, Cell Surface,Proteins, Integral Membrane,Proteins, Membrane,Proteins, Membrane-Associated,Proteins, Surface,Surface Protein, Cell
D010963	Plasmodium falciparum	A species of protozoa that is the causal agent of falciparum malaria (MALARIA, FALCIPARUM). It is most prevalent in the tropics and subtropics.	Plasmodium falciparums,falciparums, Plasmodium
D004910	Erythrocyte Membrane	The semi-permeable outer structure of a red blood cell. It is known as a red cell 'ghost' after HEMOLYSIS.	Erythrocyte Ghost,Red Cell Cytoskeleton,Red Cell Ghost,Erythrocyte Cytoskeleton,Cytoskeleton, Erythrocyte,Cytoskeleton, Red Cell,Erythrocyte Cytoskeletons,Erythrocyte Ghosts,Erythrocyte Membranes,Ghost, Erythrocyte,Ghost, Red Cell,Membrane, Erythrocyte,Red Cell Cytoskeletons,Red Cell Ghosts
D006021	Glycophorins	The major sialoglycoprotein of human erythrocyte membranes. It consists of at least two sialoglycopeptides and is composed of 60% carbohydrate including sialic acid and 40% protein. It is involved in a number of different biological activities including the binding of MN blood groups, influenza viruses, kidney bean phytohemagglutinin, and wheat germ agglutinin.	Erythrocyte Sialoglycoproteins,Glycoconnectin,Glycoconnectins,Glycophorin,Glycophorin D,MN Sialoglycoprotein,Red Blood Cell Membrane Sialoglycoprotein,Glycophorin A,Glycophorin A(M),Glycophorin B,Glycophorin C,Glycophorin E,Glycophorin HA,Ss Erythrocyte Membrane Sialoglycoproteins,Ss Sialoglycoprotein,beta-Sialoglycoprotein,Sialoglycoprotein, MN,Sialoglycoprotein, Ss,Sialoglycoproteins, Erythrocyte,beta Sialoglycoprotein
D006801	Humans	Members of the species Homo sapiens.	Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D001287	Attachment Sites, Microbiological	Specific loci on both the bacterial DNA (attB) and the phage DNA (attP) which delineate the sites where recombination takes place between them, as the phage DNA becomes integrated (inserted) into the BACTERIAL DNA during LYSOGENY.	Attachment Sites (Microbiology),Bacterial Attachment Sites,Phage Attachment Sites,Att Attachment Sites,AttB Attachment Sites,AttP Attachment Sites,Attachment Site (Microbiology),Attachment Site, Bacterial,Attachment Sites, Bacterial,Bacterial Attachment Site,Microbiologic Attachment Site,Microbiologic Attachment Sites,Att Attachment Site,AttB Attachment Site,AttP Attachment Site,Attachment Site, Att,Attachment Site, AttB,Attachment Site, AttP,Attachment Site, Microbiologic,Attachment Site, Microbiological,Attachment Site, Phage,Attachment Sites, Att,Attachment Sites, AttB,Attachment Sites, AttP,Attachment Sites, Microbiologic,Attachment Sites, Phage,Microbiological Attachment Site,Microbiological Attachment Sites,Phage Attachment Site
D001457	Anion Exchange Protein 1, Erythrocyte	A major integral transmembrane protein of the ERYTHROCYTE MEMBRANE. It is the anion exchanger responsible for electroneutral transporting in CHLORIDE IONS in exchange of BICARBONATE IONS allowing CO2 uptake and transport from tissues to lungs by the red blood cells. Genetic mutations that result in a loss of the protein function have been associated with type 4 HEREDITARY SPHEROCYTOSIS.	Anion Transport Protein, Erythrocyte,Band 3 Protein,Erythrocyte Anion Transport Protein,Erythrocyte Membrane Band 3 Protein,AE1 Anion Exchanger,AE1 Chloride-Bicarbonate Exchanger,AE1 Cl- HCO3- Exchanger,AE1 Gene Product,Anion Exchanger 1,Antigens, CD233,Band 3 Anion Transport Protein,Band III Protein,CD233 Antigen,CD233 Antigens,Capnophorin,EPB3 Protein,Erythrocyte Anion Exchanger,Erythrocyte Membrane Anion Transport Protein,Erythrocyte Membrane Protein Band 3, Diego Blood Group,Protein Band 3,SLC4A1 Protein,Solute Carrier Family 4 Member 1,Solute Carrier Family 4, Anion Exchanger, Member 1,AE1 Chloride Bicarbonate Exchanger,AE1 Cl HCO3 Exchanger,Anion Exchanger, Erythrocyte,Antigen, CD233,Chloride-Bicarbonate Exchanger, AE1,Exchanger 1, Anion,Protein, EPB3