期刊
PLOS BIOLOGY
卷 6, 期 6, 页码 1195-1207出版社
PUBLIC LIBRARY SCIENCE
DOI: 10.1371/journal.pbio.0060131
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资金
- NIAID NIH HHS [R01 AI061598, R01 AI072504, R01 AI071204, R01 AI072504-01, R01 AI071204-04, F31 AI061840] Funding Source: Medline
- NIGMS NIH HHS [T32 GM008326] Funding Source: Medline
Diversity-generating retroelements (DGRs) recognize novel ligands through massive protein sequence variation, a property shared uniquely with the adaptive immune response. Little is known about how recognition is achieved by DGR variable proteins. Here, we present the structure of the Bordetella bacteriophage DGR variable protein major tropism determinant (Mtd) bound to the receptor pertactin, revealing remarkable adaptability in the static binding sites of Mtd. Despite large dissimilarities in ligand binding mode, principles underlying selective recognition were strikingly conserved between Mtd and immunoreceptors. Central to this was the differential amplification of binding strengths by avidity (i.e., multivalency), which not only relaxed the demand for optimal complementarity between Mtd and pertactin but also enhanced distinctions among binding events to provide selectivity. A quantitatively similar balance between complementarity and avidity was observed for Bordetella bacteriophage DGR as occurs in the immune system, suggesting that variable repertoires operate under a narrow set of conditions to recognize novel ligands.
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