Modeling the Architecture of Depolymerase-Containing Receptor Binding Proteins in Klebsiella Phages

Klebsiella pneumoniae carries a thick polysaccharide capsule. This highly variable chemical structure plays an important role in its virulence. Many Klebsiella bacteriophages recognize this capsule with a receptor binding protein (RBP) that contains a depolymerase domain. This domain degrades the ca...

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Main Authors: Agnieszka Latka, Petr G. Leiman, Zuzanna Drulis-Kawa, Yves Briers
Format: Article
Language:English
Published: Frontiers Media S.A. 2019-11-01
Series:Frontiers in Microbiology
Subjects:
Online Access:https://www.frontiersin.org/article/10.3389/fmicb.2019.02649/full
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author Agnieszka Latka
Agnieszka Latka
Petr G. Leiman
Zuzanna Drulis-Kawa
Yves Briers
author_facet Agnieszka Latka
Agnieszka Latka
Petr G. Leiman
Zuzanna Drulis-Kawa
Yves Briers
author_sort Agnieszka Latka
collection DOAJ
description Klebsiella pneumoniae carries a thick polysaccharide capsule. This highly variable chemical structure plays an important role in its virulence. Many Klebsiella bacteriophages recognize this capsule 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 11 RBPs with depolymerase activity and a broad host spectrum have been identified. A detailed bioinformatic analysis shows that similar RBP domains repeatedly occur in K. pneumoniae phages with 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 an autocleavable 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 to model a set of conserved RBP architectures, indicating evolutionary linkages.
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spelling doaj.art-bb2ffbeb6b62480f8469206af784e14d2022-12-21T20:36:09ZengFrontiers Media S.A.Frontiers in Microbiology1664-302X2019-11-011010.3389/fmicb.2019.02649484384Modeling the Architecture of Depolymerase-Containing Receptor Binding Proteins in Klebsiella PhagesAgnieszka Latka0Agnieszka Latka1Petr G. Leiman2Zuzanna Drulis-Kawa3Yves Briers4Laboratory of Applied Biotechnology, Department of Biotechnology, Ghent University, Ghent, BelgiumDepartment of Pathogen Biology and Immunology, Institute of Genetics and Microbiology, University of Wrocław, Wrocław, PolandSealy Center for Structural Biology and Molecular Biophysics, Department of Biochemistry and Molecular Biology, The University of Texas Medical Branch, Galveston, TX, United StatesDepartment of Pathogen Biology and Immunology, Institute of Genetics and Microbiology, University of Wrocław, Wrocław, PolandLaboratory of Applied Biotechnology, Department of Biotechnology, Ghent University, Ghent, BelgiumKlebsiella pneumoniae carries a thick polysaccharide capsule. This highly variable chemical structure plays an important role in its virulence. Many Klebsiella bacteriophages recognize this capsule 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 11 RBPs with depolymerase activity and a broad host spectrum have been identified. A detailed bioinformatic analysis shows that similar RBP domains repeatedly occur in K. pneumoniae phages with 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 an autocleavable 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 to model a set of conserved RBP architectures, indicating evolutionary linkages.https://www.frontiersin.org/article/10.3389/fmicb.2019.02649/fullhorizontal transfertail fiber genesreceptor binding proteinphage evolutiondepolymerase
spellingShingle Agnieszka Latka
Agnieszka Latka
Petr G. Leiman
Zuzanna Drulis-Kawa
Yves Briers
Modeling the Architecture of Depolymerase-Containing Receptor Binding Proteins in Klebsiella Phages
Frontiers in Microbiology
horizontal transfer
tail fiber genes
receptor binding protein
phage evolution
depolymerase
title Modeling the Architecture of Depolymerase-Containing Receptor Binding Proteins in Klebsiella Phages
title_full Modeling the Architecture of Depolymerase-Containing Receptor Binding Proteins in Klebsiella Phages
title_fullStr Modeling the Architecture of Depolymerase-Containing Receptor Binding Proteins in Klebsiella Phages
title_full_unstemmed Modeling the Architecture of Depolymerase-Containing Receptor Binding Proteins in Klebsiella Phages
title_short Modeling the Architecture of Depolymerase-Containing Receptor Binding Proteins in Klebsiella Phages
title_sort modeling the architecture of depolymerase containing receptor binding proteins in klebsiella phages
topic horizontal transfer
tail fiber genes
receptor binding protein
phage evolution
depolymerase
url https://www.frontiersin.org/article/10.3389/fmicb.2019.02649/full
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