Structural basis of bacteriophage T5 infection trigger and
These structures bring out the important conformational changes undergone by T5 tail tip upon infection, which include bending of T5 central fiber on the side of the
Fiberless
Tail
Fiber
Structures of Mature and Urea-Treated Empty Bacteriophage T5
Thus, as with the fiberless Lambda, T5′s side tail fibers may not be essential for the host–virus interaction to trigger the DNA release. T5 lacking side tail fibers may employ a distinct
RCSB PDB
However, the in situ high-resolution structure of the neck-tail complex of siphophages remains unknown. Here, we present the structure of the
Design and Crystal Structure of Bacteriophage T4 Mini-Fibritin NCCF
Fibritin is a fibrous protein that forms “whiskers” attached to the neck of bacteriophage T4. Whiskers interact with the long tail fibers regulating the assembly and infectivity of the virus. The
RCSB PDB
Double-stranded DNA bacteriophages package their genome at high pressure inside a procapsid through the portal, an oligomeric ring protein located
Assembly and attachment of bacteriophage T4 tail fibers
Tail fiber attachment was followed by the appearance of infectious virus in mixtures of purified fiberless particles and crude extracts containing tail fibers as previously described (10).
Attachment of tail fibers in bacteriophage T4 assembly
A phage-neutralizing rabbit antiserum collected after immunization with tail-fiberless bacteriophage T4 particles was adsorbed with complete T4 phage. The resulting adsorbed serum
Evaluating Phage Tail Fiber Receptor-Binding Proteins Using
While this manuscript only demonstrates our assay''s ability to characterize adsorptive capabilities of phage tail fibers, our assay could feasibly be modified to evaluate other adsorption
Nearly complete structure of bacteriophage DT57C reveals
Here, we present the structure of DT57C determined by cryo-EM, and an atomic model of the virus, which was further explored using all-atom molecular dynamics simulations.
Podoviridae
Podoviridae Viruses of this family present short simple tails that are assembled directly into the viral head and attached to the portal by the adapter protein. Most of the known Podoviridae tail structures
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A comprehensive catalogue of receptor-binding domains in
These fibers can be categorized by five new N-terminal domains responsible for tail fiber attachment to eCIS baseplates.
8K35: Structure of the bacteriophage lambda tail tip
Here, we present the structure of the siphophage lambda "wild type," the most widely used, laboratory-adapted fiberless mutant. The neck-tail
Structure of the siphophage neck–Tail complex
Here, we present the structure of the siphophage lambda “wild type,” the most widely used, laboratory-adapted fiberless mutant. The neck–tail
Morphogenesis of the T4 tail and tail fibers
In the absence of the fibritin, the long tail fibers attach to fiberless particles very slowly. The whiskers are also be involved in the retraction of the long tail fibers under unfavorable conditions.
The Bacteriophage T7 Virion
95% of the wild-type T7 prepared for this study tail are six fibers, trimers of gp17. Each fiber has an N-terminal domain made infective centers in exponentially growing cells within 2-3 min, that attaches
Attachment of tail fibers in bacteriophage T4 assembly: Role of the
In vitro, infected-cell extracts that contain tail fibers activate whiskerless (wac) tail fiberless particles and ordinary (wac+) tail fiberless particles at equal rates if the extracts contain the wac+
RBPseg: Toward a complete phage tail fiber structure atlas
Here, we introduce RBPseg, a method that combines monomeric ESMFold predictions with a structural-based domain identification approach, to divide tail fiber sequences into manageable
Understanding Bacteriophage Tail Fiber
The exact mechanisms of how the tail fiber interacts with the receptor at the molecular/atomic level are critical for engineering phages with reprogrammed host ranges. The advancement of technologies
Structure of the siphophage neck Tail complex suggests that
Here, we present the structure of the siphophage lambda “wild type,” the most widely used, laboratory-adapted fiberless mutant. The neck–tail complex comprises a channel formed by
Visualizing Adsorption of Cyanophage P-SSP7 onto Marine
A fiberless P-SSP7 mutant has not been studied; however, tail fiber conformations seem to exert the same function in adsorption as those in other bacteriophages.
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