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PMID:17557882
| Citation |
Southern, TR, Jolly, CE, Lester, ME and Hayman, JR (2007) EnP1, a microsporidian spore wall protein that enables spores to adhere to and infect host cells in vitro. Eukaryotic Cell 6:1354-62 |
|---|---|
| Abstract |
Microsporidia are spore-forming fungal pathogens that require the intracellular environment of host cells for propagation. We have shown that spores of the genus Encephalitozoon adhere to host cell surface glycosaminoglycans (GAGs) in vitro and that this adherence serves to modulate the infection process. In this study, a spore wall protein (EnP1; Encephalitozoon cuniculi ECU01_0820) from E. cuniculi and Encephalitozoon intestinalis is found to interact with the host cell surface. Analysis of the amino acid sequence reveals multiple heparin-binding motifs, which are known to interact with extracellular matrices. Both recombinant EnP1 protein and purified EnP1 antibody inhibit spore adherence, resulting in decreased host cell infection. Furthermore, when the N-terminal heparin-binding motif is deleted by site-directed mutagenesis, inhibition of adherence is ablated. Our transmission immunoelectron microscopy reveals that EnP1 is embedded in the microsporidial endospore and exospore and is found in high abundance in the polar sac/anchoring disk region, an area from which the everting polar tube is released. Finally, by using a host cell binding assay, EnP1 is shown to bind host cell surfaces but not to those that lack surface GAGs. Collectively, these data show that given its expression in both the endospore and the exospore, EnP1 is a microsporidian cell wall protein that may function both in a structural capacity and in modulating in vitro host cell adherence and infection. |
| Links |
PubMed PMC1951136 Online version:10.1128/EC.00113-07 |
| Keywords |
Amino Acid Sequence; Animals; Blotting, Western; CHO Cells/parasitology; Cell Wall/chemistry; Cells, Cultured; Cercopithecus aethiops; Cricetinae; Cricetulus; Encephalitozoon/chemistry; Fungal Proteins/chemistry; Fungal Proteins/genetics; Host-Parasite Interactions/physiology; Molecular Sequence Data; Rabbits; Recombinant Proteins/chemistry; Recombinant Proteins/genetics; Sequence Alignment; Spores, Fungal/chemistry; Spores, Fungal/physiology; Vero Cells/parasitology |
| edit table |
Significance
Annotations
| Gene product | Qualifier | GO Term | Evidence Code | with/from | Aspect | Extension | Notes | Status |
|---|---|---|---|---|---|---|---|---|
|
part_of |
GO:0031160: spore wall |
ECO:0000314: direct assay evidence used in manual assertion |
C |
Seeded From UniProt |
complete | |||
| GO:0031160: spore wall |
ECO:0000314: |
C |
Figure 5b: Cells infected with E. cuniculi were incubated with EnP1 antibody, a secondary antibody was conjugated with gold, gold particles were found on exospore (outer spore wall) of mature E. cuniculi spores |
complete | ||||
| GO:0005539: glycosaminoglycan binding |
ECO:0000314: |
F |
Figure 9: Recombinant EnP1 bound to Vero and CHO cells (Vero+, CHO+), did not bind to mutant CHO cells lacking surface glycosaminoglycan (pgsA-745, pgsD-677) |
complete | ||||
| GO:0031160: spore wall |
ECO:0000314: |
C |
Figure 5d: Cells infected with E. intestinalis were incubated with EnP1 antibody, a secondary antibody was conjugated with gold, gold particles were found on exospore (outer spore wall) of mature E. intestinalis spores |
complete | ||||
|
part_of |
GO:0031160: spore wall |
ECO:0000314: direct assay evidence used in manual assertion |
C |
Seeded From UniProt |
complete | |||
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