ArticleScientific reports2017
Tail tubular protein A: a dual-function tail protein of Klebsiella pneumoniae bacteriophage KP32.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 46 citations in OpenAlex.
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- The N-Terminal Domain of Tailspike Depolymerases Affects the Replication Efficiency of SyntheticInternational journal of molecular sciences · 2025Article
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- The non-nutritive sweetener rebaudioside a enhances phage infectivity.Scientific reports · 2025Article
- Bacteriophage therapy: a possible alternative therapy against antibiotic-resistant strains ofFrontiers in microbiology · 2025Review
- Intestinal dysbiosis associated with non-nutritive sweeteners intake: an effect without a cause?Frontiers in nutrition · 2025Review
- Targeting Pseudomonas aeruginosa biofilm with an evolutionary trained bacteriophage cocktail exploiting phage resistance trade-offs.Nature communications · 2024Article
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- Phage therapy of antibiotic-resistant strains of Klebsiella pneumoniae, opportunities and challenges from the past to the future.Folia microbiologica · 2023Review
- A NewMicroorganisms · 2022Article
- Tail proteins of phage SU10 reorganize into the nozzle for genome delivery.Nature communications · 2022Article
- Bacteriophage Tail Proteins as a Tool for Bacterial Pathogen Recognition-A Literature Review.Antibiotics (Basel, Switzerland) · 2022Review
- Potential application of a newly isolated phage BUCT609 infectingFrontiers in microbiology · 2022Article
- Characterization and Full Genome Sequence of Novel KPP-5 Lytic Phage againstBiomedicines · 2021Article
- Characterization of four virulent Klebsiella pneumoniae bacteriophages, and evaluation of their potential use in complex phage preparation.Virology journal · 2021Article
- Characteristics of a Bacteriophage, vB_Kox_ZX8, Isolated From ClinicalFrontiers in microbiology · 2021Article
Corrections and comments
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Authors and funding
6 authors at 5 institutions in 2 countries.
Funding
Abstract
Tail tubular protein A (TTPA) is a structural tail protein of Klebsiella pneumoniae bacteriophage KP32, and is responsible for adhering the bacteriophage to host cells. For the first time, we found that TTPA also exhibits lytic activity towards capsular exopolysaccharide (EPS) of the multiresistant clinical strain of Klebsiella pneumoniae, PCM2713, and thus should be regarded as a dual-function macromolecule that exhibits both structural and enzymatic actions. Here, we present our crystallographic and enzymatic studies of TTPA. TTPA was crystallized and X-ray diffraction data were collected to a resolution of 1.9 Å. In the crystal, TTPA molecules were found to adopt a tetrameric structure with α-helical domains on one side and β-strands and loops on the other. The novel crystal structure of TTPA resembles those of the bacteriophage T7 tail protein gp11 and gp4 of bacteriophage P22, but TTPA contains an additional antiparallel β-sheet carrying a lectin-like domain that could be responsible for EPS binding. The enzymatic activity of TTPA may reflect the presence of a peptidoglycan hydrolase domain in the α-helical region (amino acid residues 126 to 173). These novel results provide new insights into the enzymatic mechanism through which TTPA acts on polysaccharides.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.