期刊
MICROBIAL BIOTECHNOLOGY
卷 13, 期 6, 页码 1765-1779出版社
WILEY
DOI: 10.1111/1751-7915.13593
关键词
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资金
- Science Foundation Ireland (SFI) [15/SIRG/3430]
- SFI [13/IA/1953]
- French Infrastructure for Integrated Structural Biology (FRISBI) [ANR-10-INSB-0501]
Available 3D structures of bacteriophage modules combined with predictive bioinformatic algorithms enabled the identification of adhesion modules in 57 siphophages infectingStreptococcus thermophilus(St). We identified several carbohydrate-binding modules (CBMs) in so-called evolved distal tail (Dit) and tail-associated lysozyme (Tal) proteins of St phage baseplates. We examined the open reading frame (ORF) downstream of the Tal-encoding ORF and uncovered the presence of a putative p2-like receptor-binding protein (RBP). A 21 angstrom resolution electron microscopy structure of the baseplate ofcos-phage STP1 revealed the presence of six elongated electron densities, surrounding the core of the baseplate, that harbour the p2-like RBPs at their tip. To verify the functionality of these modules, we expressed GFP- or mCherry-coupled Tal and putative RBP CBMs and observed by fluorescence microscopy that both modules bind to their corresponding St host, the putative RBP CBM with higher affinity than the Tal-associated one. The large number of CBM functional domains in St phages suggests that they play a contributory role in the infection process, a feature that we previously described in lactococcal phages and beyond, possibly representing a universal feature of the siphophage host-recognition apparatus.
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