Hemolysis or haemolysis, also known by several other names, is the rupturing (lysis) of red blood cells (erythrocytes) and the release of their contents (cytoplasm) into surrounding fluid. Hemolysis may occur in vivo or in vitro.
Lysis refers to the breaking down of the membrane of a cell, often by viral, enzymic, or osmotic mechanisms that compromise its integrity. A fluid containing the contents of lysed cells is called a lysate. In molecular biology, biochemistry, and cell biology laboratories, cell cultures may be subjected to lysis in the process of purifying their components, as in protein purification, DNA extraction, RNA extraction, or in purifying organelles.
A lysis buffer is a buffer solution used for the purpose of breaking open cells for use in molecular biology experiments that analyze the labile macromolecules of the cells. Most lysis buffers contain buffering salts and ionic salts to regulate the pH and osmolarity of the lysate. Sometimes detergents are added to break up membrane structures. For lysis buffers targeted at protein extraction, protease inhibitors are often included, and in difficult cases may be almost required. Lysis buffers can be used on both animal and plant tissue cells.
Tumor lysis syndrome is a group of metabolic abnormalities that can occur as a complication during the treatment of cancer, where large amounts of tumor cells are killed off (lysed) at the same time by the treatment, releasing their contents into the bloodstream. This occurs most commonly after the treatment of lymphomas and leukemias. In oncology and hematology, this is a potentially fatal complication, and patients at increased risk for TLS should be closely monitored before, during, and after their course of chemotherapy.
The lytic cycle is one of the two cycles of viral reproduction, the other being the lysogenic cycle. The lytic cycle results in the destruction of the infected cell and its membrane. Bacteriophages that only use the lytic cycle are called virulent phages.
Cytolysis, or osmotic lysis, occurs when a cell bursts due to an osmotic imbalance that has caused excess water to diffuse into the cell. Water can enter the cell by diffusion through the cell membrane or through selective membrane channels called aquaporins, which greatly facilitate the flow of water. It occurs in a hypotonic environment, where water moves into the cell by osmosis and causes its volume to increase to the point where the volume exceeds the membrane's capacity and the cell bursts. The presence of a cell wall prevents the membrane from bursting, so cytolysis only occurs in animal and protozoa cells which do not have cell walls. The reverse process is plasmolysis.
Leviviridae is a family of viruses. Bacteria, including Enterobacteria, Caulobacter, Pseudomonas, and Acinetobacter serve as natural hosts for these bacteriophages. There are currently four species in this family, divided among 2 genera. They are small RNA viruses with linear, positive-sense, single-stranded RNA genomes that encode only four proteins. All phages of this family require bacterial pili to attach to and infect cells.
Lysins, also known as endolysins or murein hydrolases, are hydrolytic enzymes produced by bacteriophages in order to cleave the host's cell wall during the final stage of the lytic cycle. Lysins are highly evolved enzymes that are able to target one of the five bonds in peptidoglycan (murein), the main component of bacterial cell walls, which allows the release of progeny virions from the lysed cell. Cell-wall-containing Archaea are also lysed by specialized pseudomurein-cleaving lysins, while most archaeal viruses employ alternate mechanisms. Similarly, not all bacteriophages synthesize lysins: some small single-stranded DNA and RNA phages produce membrane proteins that activate the host's autolytic mechanisms.
Holins are a diverse group of small proteins produced by dsDNA bacteriophages in order to trigger and control the degradation of the host's cell wall at the end of the lytic cycle. Holins form pores in the host's cell membrane, allowing lysins to reach and degrade peptidoglycan, a component of bacterial cell walls. Holins have been shown to regulate the timing of lysis with great precision. Over 50 unrelated gene families encode holins, making them the most diverse group of proteins with common function. Together with lysins, holins are being studied for their potential use as antibacterial agents.
The Holin superfamily II is a superfamily of putative pore-forming proteins. It is one of the seven different holin superfamilies in total. In general, these proteins are thought to play a role in regulated cell death, although functionality varies between families and individual members. The Holin superfamily II includes the TC families:
The LydA Holin Family, named after the lydA gene which codes for its prototype member, belongs to the Holin Superfamily III. Members of this family have 3 transmembrane segments (TMSs) and appear to possess between 90 and 120 amino acyl residues (aas). A representative list of proteins belonging to this family can be found in the Transporter Classification Database.
The Pseudomonas aeruginosa Hol Holin Family is a group of transporters belonging to the Holin Superfamily III.
The Bacillus subtilis φ29 Holin Family is a group of transporters belonging to the Holin Superfamily IV. A representative list of members belonging to the φ29 holin family can be found in the Transporter Classification Database.
The Cph1 Holin Family is also called the CDD Holin 4 superfamily, but belongs to the Holin Superfamily IV as classified in the Transporter Classification Database (TCDB). A representative list of members belonging to the Cph1 family can be found in TCDB.
The Listeria Phage A118 Holin (Hol118) Family is a group of transporters belonging to the Holin Superfamily V. A representative list of proteins belonging to the Hol118 family can be found in the Transporter Classification Database.
The Mycobacterial 2 TMS Phage Holin Family is a group of transporters belonging to the Holin Superfamily VII. The Mycobactrerial 2 transmembrane segment (TMS) Holins have been identified and recognized by Catalao et al (2012). The Mycobacterium phage D29 gp11 protein is a holin that, upon expression, rapidly kills both E. coli and Mycobacterium smegmatis. Shortening gp11 from its C-terminus resulted in diminished cytotoxicity and smaller holes. The two TMSs at the N-terminus alone do not integrate into the cytoplasmic membrane and do not show toxicity. Fusion of the two TMSs and a small C-terminal coiled-coil region resulted in restoration of cell killing. The second TMS is dispensable for toxicity. The gp11 C-terminal region is therefore necessary but not sufficient for toxicity.
The Lactococcus lactis Phage r1t Holin Family is a family of putative pore-forming proteins that typically range in size between about 65 and 95 amino acyl residues (aas) in length, although a few r1t holins have been found to be significantly larger. Phage r1t holins exhibit between 2 and 4 transmembrane segments (TMSs), with the 4 TMS proteins resulting from an intragenic duplication of a 2 TMS region. A representative list of the proteins belonging to the r1t holin family can be found in the Transporter Classification Database.
Gene transfer agent-release holins are holins which are believed to facilitate the lysis-dependent release of a gene transfer agent. Particularly the gene transfer agent of Rhodobacter capsulatus (RcGTA), which is known to be a bacteriophage-like genetic element that induces horizontal gene transfer. The promoter of the RcGTA gene was identified by Westbye et al. in 2013. A representative list of members belonging to the GTA-Hol family can be found in the Transporter Classification Database with homologues found in proteobacteria and caudovirales.
The Putative Holin-2 (PH-2) Family is a large family with members from a wide variety of bacteria. As of early 2016, functional data is not available for members of the PH-2 family, but based on their size and topology, it is believed they act as holins to facilitate cell lysis. PH-2 family proteins are of 130 to 210 amino acyl residues (aas) in length and may exhibit 1 or 2 transmembrane segments (TMSs). A representative list of proteins belonging to the PH-2 family can be found in the Transporter Classification Database.
