Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
7
pubmed:dateCreated
2004-2-9
pubmed:abstractText
In Plasmodium falciparum malaria, erythrocyte invasion by circulating merozoites may occur via two distinct pathways involving either a sialic acid-dependent or -independent mechanism. Earlier, we identified two nonglycosylated exofacial regions of erythrocyte band 3 termed 5ABC and 6A as an important host receptor in the sialic acid-independent invasion pathway. 5ABC, a major segment of this receptor, interacts with the 42-kDa processing product of merozoite surface protein 1 (MSP1(42)) through its 19-kDa C-terminal domain. Here, we show that two regions of merozoite surface protein 9 (MSP9), also known as acidic basic repeat antigen, interact directly with 5ABC during erythrocyte invasion by P. falciparum. Native MSP9 as well as recombinant polypeptides derived from two regions of MSP9 (MSP9/Delta1 and MSP9/Delta2) interacted with both 5ABC and intact erythrocytes. Soluble 5ABC added to the assay mixture drastically diminished the binding of MSP9 to erythrocytes. Recombinant MSP9/Delta1 and MSP9/Delta2 present in the culture medium blocked P. falciparum reinvasion into erythrocytes in vitro. Native MSP9 and MSP1(42), the two ligands binding to the 5ABC receptor, existed as a stable complex. Our results establish a novel concept wherein the merozoite exploits a specific complex of co-ligands on its surface to target a single erythrocyte receptor during invasion. This new paradigm poses a new challenge in the development of a vaccine for blood stage malaria.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Anion Exchange Protein 1..., http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Culture Media, http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary, http://linkedlifedata.com/resource/pubmed/chemical/Ligands, http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Protozoan Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins, http://linkedlifedata.com/resource/pubmed/chemical/erythrocyte binding protein-2..., http://linkedlifedata.com/resource/pubmed/chemical/merozoite surface protein 9...
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
13
pubmed:volume
279
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
5765-71
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:14630931-Animals, pubmed-meshheading:14630931-Anion Exchange Protein 1, Erythrocyte, pubmed-meshheading:14630931-Blotting, Western, pubmed-meshheading:14630931-Carrier Proteins, pubmed-meshheading:14630931-Culture Media, pubmed-meshheading:14630931-DNA, Complementary, pubmed-meshheading:14630931-Dose-Response Relationship, Drug, pubmed-meshheading:14630931-Erythrocytes, pubmed-meshheading:14630931-Gene Library, pubmed-meshheading:14630931-Humans, pubmed-meshheading:14630931-Ligands, pubmed-meshheading:14630931-Membrane Proteins, pubmed-meshheading:14630931-Models, Biological, pubmed-meshheading:14630931-Plasmodium falciparum, pubmed-meshheading:14630931-Precipitin Tests, pubmed-meshheading:14630931-Protein Binding, pubmed-meshheading:14630931-Protein Structure, Tertiary, pubmed-meshheading:14630931-Protozoan Proteins, pubmed-meshheading:14630931-Recombinant Fusion Proteins, pubmed-meshheading:14630931-Recombinant Proteins, pubmed-meshheading:14630931-Two-Hybrid System Techniques
pubmed:year
2004
pubmed:articleTitle
A co-ligand complex anchors Plasmodium falciparum merozoites to the erythrocyte invasion receptor band 3.
pubmed:affiliation
Division of Cell Biology, Caritas St. Elizabeth's Medical Center, Tufts University School of Medicine, Boston, Massachusetts 02135, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't