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Tail Of The Bacteriophages

the bacteriophage entity very present in the earth,is composed of a tail that can be of various types that allows the entity to recognize the host and deliver the DNA from the capsid to the cytoplasm of the infected cell regardless of their gram positive or gram negative host, or their receptor nature or the type of polysaccharide or protein surface in fact the central tail architecture of all caudophages and phage derivates, the systems share the same structural organization and are believed to be be homologous.
here we review recent advances in the structure, function and assembly of the phage tail architecture.
in fact, we have three categories of the phages also classified according to the type of tail, such as siphovoridae (long flexible tail) then myoviridae (long contractual tail) and podovoridae (short tail). The path to mount the capsid and also the tail are indipendent. The capsids full of DNA with the tails assembling form the complete virion, which is released with cell lysis.
Because there is an interaction with the cell surface, there is a trigger for infection in the host cell. The phage tail is still a highly sought after and interesting subject of study especially in terms of perforation of the cell wall, in fact the tail has precisely the task of the delivering the genome into the bacterium cytoplasm. So the tail is a multy-protein and complex structure that mediates the expulsion of the genome, little is known about how the tail can pass through the last layer that protects the cytoplasm of the host cell, images from cryoelectric microscopy (cryo-em) show that phages use the tail to form a pore through which the genome enters the bacterial cell.

SIPHOPHAGE TAIL ANALYSIS

thus at its distal end, the tip of the tail complex is equipped with receptor-bound proteins (RBP),which are more present in one or more copies and tail fibers may also be present in siphophages. The core of the tail complex is formed by a ring of the hexameric protein of the distal tail protein (DTP), and a trimeric ring of the "HUB" protein of the baseplate (BHP), Then we have in the proximal side a long tube formed by oligomerization of the tail tube protein (TTP) around the (TMP) tape measure protein.
This tube ends with the terminator protein or in some cases the completion protein. In myophages the tail is wrapped in a sheath.

Tail Assembly Of The SIPHOPHAGES

During tail assembly, the long TMP is stabilized by the chaperones and in most phages,two proteins named by IG and GT, are synthesized and via a programmed translational frameshift -1. The effectiveness of frameshift determines the ratio of G/GT which has been shown to be a crucial for proper tail assembly. Structural analyzes suggest that G coils the TMP in a spiral mode. the polymerization of TTP around the TMP has also been demonstred which would transform the TTP into an oligomerization core. It has been explained that the TMp is folden into the tail tube in a metastable conformation, which would relax after host binding, into a lower energy conformation leading to facilitated ejection from the tail and expulsion of TMP would trigger the release of DNA from the capsid. C-terminal proteomysis could induce a transition from a chaperone bound state to a metastable TTP.
the tail tip complex located at the distal end of the tail,the tip complex is the fagus guest recogniton apparatus .although very different in size and shape, from large base plate-like sructures to very small ones, the tip comprises two structurally conserved proteins, BHP or TAL and DTP or DIT, which are also the nucleos of the phages and system of injection beat us related phages. The tip complex acts as the HUB for the RBP, or at the end of the central fiber. Over the past decade, several structures of the siphophagus tip have become available, often through a combination of EM and X-ray crystallography. for example in the "p2" phages the central role of the DTP/BHP oligomerization and assembly together with the TMP/TAC complex,which appears to be the initiator complex. The assembly of the initiator complex is followed by the polymerization of the TTP to form a tube and the attachment of peripheral proteins to the base plate . The RBPs were made developed to adapt to very different cell surfaces from the hosts.

TAIL OF THE SIPHOVIRIDAE CATEGORY

The long tail of this type of phages acts as a molecular machine that expels viral DNA from the capsid into the host cell's cytoplasm. The ejection system is made up of a central tube, base plate and a terminator assembly that fixes the tail of the phage capsid. After having bonded to the surface the baseplate with coformation and triggers expulsion of the genome in the cytoplasm of the host cell, it is said that the source of the forces that causes the expulsion of the viral genome to be due to an osmotic pressure imbalance between the virus and the interior of the host cytoplasm.

way to prenetrate in gram positive and gram negative bacteria

GRAM POSITIVE: among the phages of the siphages we have the attachment to a receptor of the outer membrane of the cell that is infected, the tip of the tail penetrates the OM of the host and the exolysin attached to the virion (if present) hydrolyzes the peptydoglycan state. the tail reaches the host's plasma membrane, through which a pore opens for the translocation of viral DNA.
GRAM NEGATIVE: Attachment to a host cell wall receptor occurs and hydrolysis is associeted with the tip of the peptydoglyca layer. The tail reaches the plasma membrane of the infected cell and a loss of the tip is possible with subsequent opening of the cap and use of a hydrophilic pore for the translocation of viable DNA into the host cytoplasm.

Note

^[1] ^[2] ^[3] ^[2] ^[4]

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