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Modelling the Architecture of Depolymerase-Containing Receptor Binding Proteins in Klebsiella phages

(2019)
Author
Organization
Abstract
Klebsiella pneumoniae carries a thick and diverse polysaccharide capsule that plays an important role in its virulence. Many Klebsiella bacteriophages recognize this substrate with a receptor binding protein (RBP) that contains a depolymerase domain. This domain degrades the capsule to initiate phage infection. RBPs are highly specific and thus largely determine the host spectrum of the phage. A majority of known Klebsiella phages have only one or two RBPs, but phages with up to eleven RBPs with depolymerase activity and a broad host spectrum have been identified. A detailed bioinformatic analysis shows that Klebsiella phages extensively recycle structural RBP domains for attachment of an RBP to the phage tail (anchor domain) or for branching of RBPs (T4gp10-like domain). Structural domains determining the RBP architecture are located at the N-terminus, while the depolymerase is located in the center of protein. Occasionally, the RBP is complemented with a chaperone domain at the distal end serving for folding and multimerization. The enzymatic domain is subjected to an intense horizontal transfer to rapidly shift the phage host spectrum without affecting the RBP architecture. These analyses allowed us to model a set of conserved RBP architectures that are not limited to taxonomic borders, indicating evolutionary linkages.
Keywords
Phage, Klebsiella, depolymerase

Citation

Please use this url to cite or link to this publication:

Chicago
Łątka, Agnieszka, Petr G. Leiman, Zuzanna Drulis-Kawa, and Yves Briers. 2019. “Modelling the Architecture of Depolymerase-Containing Receptor Binding Proteins in Klebsiella Phages.” In .
APA
Łątka, A., Leiman, P. G., Drulis-Kawa, Z., & Briers, Y. (2019). Modelling the Architecture of Depolymerase-Containing Receptor Binding Proteins in Klebsiella phages. Presented at the 23rd Biennal Evergreen International Phage Meeting.
Vancouver
1.
Łątka A, Leiman PG, Drulis-Kawa Z, Briers Y. Modelling the Architecture of Depolymerase-Containing Receptor Binding Proteins in Klebsiella phages. 2019.
MLA
Łątka, Agnieszka et al. “Modelling the Architecture of Depolymerase-Containing Receptor Binding Proteins in Klebsiella Phages.” 2019. Print.
@inproceedings{8625030,
  abstract     = {Klebsiella pneumoniae carries a thick and diverse polysaccharide capsule that plays an important role in its virulence. Many Klebsiella bacteriophages recognize this substrate with a receptor binding protein (RBP) that contains a depolymerase domain. This domain degrades the capsule to initiate phage infection. RBPs are highly specific and thus largely determine the host spectrum of the phage. A majority of known Klebsiella phages have only one or two RBPs, but phages with up to eleven RBPs with depolymerase activity and a broad host spectrum have been identified. A detailed bioinformatic analysis shows that Klebsiella phages extensively recycle structural RBP domains for attachment of an RBP to the phage tail (anchor domain) or for branching of RBPs (T4gp10-like domain). Structural domains determining the RBP architecture are located at the N-terminus, while the depolymerase is located in the center of protein. Occasionally, the RBP is complemented with a chaperone domain at the distal end serving for folding and multimerization. The enzymatic domain is subjected to an intense horizontal transfer to rapidly shift the phage host spectrum without affecting the RBP architecture. These analyses allowed us to model a set of conserved RBP architectures that are not limited to taxonomic borders, indicating evolutionary linkages.},
  author       = {Łątka, Agnieszka and Leiman, Petr G. and Drulis-Kawa, Zuzanna and Briers, Yves},
  keywords     = {Phage,Klebsiella,depolymerase},
  location     = {The Evergreen State College, Olympia, WA},
  title        = {Modelling the Architecture of Depolymerase-Containing Receptor Binding Proteins in Klebsiella phages},
  year         = {2019},
}