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Your search keyword '"Amy L. Springer"' showing total 2 results
Start Over Author "Amy L. Springer" Journal molecular microbiology
2 results on '"Amy L. Springer"'

1. Mapping a common interaction site used by Plasmodium falciparum Duffy binding-like domains to bind diverse host receptors

Author

Dasein P.-G. Howell, Emily Levin, Joseph D. Smith, Amy L. Springer, William R. Schief, David J. Phippard, and Susan M. Kraemer

Subjects
Alanine, Glycan, biology, Intercellular Adhesion Molecule-1, Mutant, Plasmodium falciparum, biology.organism_classification, Microbiology, Virology, Cell biology, Apicomplexa, Cerebral Malaria, parasitic diseases, biology.protein, Receptor, Molecular Biology
Abstract

The Duffy binding-like (DBL) domain is a key adhesive module in Plasmodium falciparum, present in both erythrocyte invasion ligands (EBLs) and the large and diverse P. falciparum erythrocyte membrane protein 1 (PfEMP1) family of cytoadherence receptors. DBL domains bind a variety of different host receptors, including intercellular adhesion molecule 1 (ICAM-1), a receptor interaction that may have a role in infected erythrocyte binding to cerebral blood vessels and cerebral malaria. In this study, we expressed the nearly full complement of DBLbeta-C2 domains from the IT4/25/5 (IT4) parasite isolate and showed that ICAM-1-binding domains (DBLbeta-C2(ICAM-1)) were confined to group B and group C PfEMP1 proteins and were not present in group A, suggesting that ICAM-1 selection pressure differs between PfEMP1 groups. To further dissect the molecular determinants of binding, we modelled a DBLbeta-C2(ICAM-1) domain on a solved DBL structure and created alanine substitution mutants in two DBLbeta-C2(ICAM-1) domains. This analysis indicates that the DBLbeta-C2::ICAM-1 interaction maps to the equivalent glycan binding region of EBLs, and suggests a general model for how DBL domains evolve under dual selection for host receptor binding and immune evasion.

Published
2007

2. Mapping a common interaction site used by Plasmodium falciparum Duffy binding-like domains to bind diverse host receptors

Author

Dasein P-G, Howell, Emily A, Levin, Amy L, Springer, Susan M, Kraemer, David J, Phippard, William R, Schief, and Joseph D, Smith

Subjects
Models, Molecular, Binding Sites, Molecular Sequence Data, Plasmodium falciparum, Protozoan Proteins, Antigens, Protozoan, Receptors, Cell Surface, Intercellular Adhesion Molecule-1, Host-Parasite Interactions, Protein Structure, Tertiary, COS Cells, Chlorocebus aethiops, Protein Interaction Mapping, Mutagenesis, Site-Directed, Animals, Amino Acid Sequence, Sequence Alignment, Sequence Analysis, Phylogeny, Protein Binding
Abstract

The Duffy binding-like (DBL) domain is a key adhesive module in Plasmodium falciparum, present in both erythrocyte invasion ligands (EBLs) and the large and diverse P. falciparum erythrocyte membrane protein 1 (PfEMP1) family of cytoadherence receptors. DBL domains bind a variety of different host receptors, including intercellular adhesion molecule 1 (ICAM-1), a receptor interaction that may have a role in infected erythrocyte binding to cerebral blood vessels and cerebral malaria. In this study, we expressed the nearly full complement of DBLbeta-C2 domains from the IT4/25/5 (IT4) parasite isolate and showed that ICAM-1-binding domains (DBLbeta-C2(ICAM-1)) were confined to group B and group C PfEMP1 proteins and were not present in group A, suggesting that ICAM-1 selection pressure differs between PfEMP1 groups. To further dissect the molecular determinants of binding, we modelled a DBLbeta-C2(ICAM-1) domain on a solved DBL structure and created alanine substitution mutants in two DBLbeta-C2(ICAM-1) domains. This analysis indicates that the DBLbeta-C2::ICAM-1 interaction maps to the equivalent glycan binding region of EBLs, and suggests a general model for how DBL domains evolve under dual selection for host receptor binding and immune evasion.

Published
2007

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