Interaction and assembly of two novel proteins in the spore wall of the microsporidian species Nosema bombycis and their roles in adherence to and infection of host cells.
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SWP7 is localized to the exospore and endospore of mature N. bombycis spores and colocalizes there with SWP9.
"Both SWP7 and SWP9 are specifically colocalized to the spore wall in mature spores."
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SWP7 interacts with SWP9, shown by four independent assays.
"immunoprecipitation, far-Western blotting, unreduced SDS-PAGE, and yeast two-hybrid data demonstrated that SWP7 interacted with SWP9"
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Recombinant SWP7 does not bind the deproteinated chitin spore coat on its own; its binding requires SWP9 to be bound first. Chitin binding is therefore not a molecular function of SWP7.
"binding of the recombinant protein rSWP7-His to the DCSCs is dependent on the combination of rSWP9-glutathione S-transferase (GST) with the DCSCs"
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Masking SWP7 on the spore surface with antibody reduces adhesion of spores to, and infection of, host cells.
"anti-SWP9, and anti-SWP7 antibodies decreased spore adhesion and infection of the host cell"
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The authors' structural claim for SWP7 is hedged, and they frame SWP9 rather than SWP7 as the scaffold.
"A possible major function of SWP9 is as a scaffolding protein that supports other proteins (such as SWP7) that form the integrated spore wall of N. bombycis"