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We found that the side tail fibers interfere with phage DNA ejection process, most likely through the binding with their receptors, OmpC, leading to a more frequent failed infection. However,
Here we present the crystal structure of the receptor-binding tip of the bacteriophage T4 long tail fiber, which is highly homologous to the tip of the
Bacteriophage tail fibers'' primary role is to locate and bind to specific receptor molecules on the surface of a susceptible bacterial host cell, initiating the infection process.
In this review, we comprehensively summarize how the tail fibers of the T4 phage recognize host surface receptors at single-molecule and atomic
Bacteriophages use receptor- binding proteins (RBPs) to adhere to bacterial hosts, yet their sequence and struc-tural diversity remain poorly understood. Tail fibers, a major class of RBPs,
Bacteriophage T4 has two sets of tail fibers, long tail fibers that are the initial receptor binding proteins and short tail fibers that bind subsequently and trigger
At the first step of phage infection, the receptor-binding proteins (RBPs) such as tail fibers are responsible for recognizing specific host surface receptors. The proper folding and assembly of
Bacteriophage infection, a pivotal process in microbiology, initiates with the phage''s tail recognizing and binding to the bacterial cell surface, which then mediates the injection of viral DNA
During this process long tail fibers have to withstand detaching forces, such as those caused by the Brownian fluctuations, the mechanical tensions derived from the multiple conformational changes
The structure resembles the receptor-binding tip from the bacteriophage T4 long tail fiber yet showing marked differences in its domain organization, size, sequence identity and metal binding
At the first step of phage infection, the receptor-binding proteins (RBPs) such as tail fibers are responsible for recognizing specific host surface
However, the interactions that govern this critical process are poorly understood. Here, we provide the first molecular description of a tail fiber tip.
Long tail fibers of bacteriophage T4 are formed by proteins gp34, gp35, gp36, and gp37, with gp34 located at the phage-proximal end and gp37 at
Here, we introduce RBPseg, a method that combines monomeric ESMFold predictions with a structural- based domain identi cation approach, to divide tail ber sequences into manageable fractions for high-
This study shows that the tail tips, the most diversified region across bacteriophage lambda and other long-tailed phages (or tail-like machines),
Bacteriophage T4 initially recognizes its host cells using its long tail fibers. Long tail fibers consist of a phage-proximal and a phage-distal rod, each around 80 nm long and attached to each
Tailed phages use a broad range of receptor-binding proteins, such as tail fibres, tail spikes and the central tail spike, to target their cognate bacterial
They contain a head (capsid), a contractile tail, and a baseplate to which six long tail fibers (LTFs) are attached. During infection, the genome
The interaction between a bacteriophage and its host is mediated by the phage''s tail fiber “tip” domain or receptor binding domain, which is thus the
The short tail fibre is hinged with the receptor-binding region hidden in the baseplate and enables binding, and it rotates and extends in a process
These hollow elongated protein structures, present in most bacteriophages of the order Caudovirales, connect the DNA-containing capsid with a receptor function at the distal end of the tail
The crystal structure of a complex between the tail fibre and tail fibre assembly (Tfa) protein of Escherichia coli phage Mu reveals the mechanisms by which Tfa regulates fibre assembly
Homology comparison and adsorption experiments confirmed that the tail fiber protein Lp35 of phage LP31 participated in the adsorption process as a