fusion protein

融合タンパク質

WordNet

1. a nuclear reaction in which nuclei combine to form more massive nuclei with the simultaneous release of energy (同)nuclear_fusion, nuclear fusion reaction
2. the merging of adjacent sounds or syllables or words
3. correction of an unstable part of the spine by joining two or more vertebrae; usually done surgically but sometimes done by traction or immobilization (同)spinal_fusion
4. the act of fusing (or melting) together
5. an occurrence that involves the production of a union (同)merger, unification
6. the combining of images from the two eyes to form a single visual percept (同)optical fusion
7. any of a large group of nitrogenous organic compounds that are essential constituents of living cells; consist of polymers of amino acids; essential in the diet of animals for growth and for repair of tissues; can be obtained from meat and eggs and milk and legumes; "a diet high in protein"

PrepTutorEJDIC

1. 〈U〉(金属などが)溶けること,融解,融合《+『of』+『名』》 / 〈C〉融合物 / 〈C〉(政党・党派などの)連合,合同;(民族などの)融合《+『of』+『名』》 / 〈U〉〈C〉核融合(nuclear fusion)
2. 蛋白(たんばく)質

Wikipedia preview

出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2015/06/24 10:32:20」(JST)

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[Wiki en表示]

This article is about chimeric fusion proteins. For proteins involved in membrane fusion, see membrane fusion protein.

Fusion proteins or chimeric proteins (literally, made of parts from different sources) are proteins created through the joining of two or more genes that originally coded for separate proteins. Translation of this fusion gene results in a single or multiple polypeptides with functional properties derived from each of the original proteins. Recombinant fusion proteins are created artificially by recombinant DNA technology for use in biological research or therapeutics. Chimeric or chimera usually designate hybrid proteins made of polypeptides having different functions or physico-chemical patterns. Chimeric mutant proteins occur naturally when a complex mutation, such as a chromosomal translocation, tandem duplication, or retrotransposition creates a novel coding sequence containing parts of the coding sequences from two different genes. Naturally occurring fusion proteins are commonly found in cancer cells, where they may function as oncoproteins. The bcr-abl fusion protein is a well-known example of an oncogenic fusion protein, and is considered to be the primary oncogenic driver of chronic myelogenous leukemia.

Functions

Some fusion proteins combine whole peptides and therefore contains all functional domains of the original proteins. However, other fusion proteins, especially those that are naturally occurring, combine only portions of coding sequences and therefore do not maintain the original functions of the parental genes that formed them.

Many whole gene fusions are fully functional, and can still act to replace the original peptides. Some, however, experience interactions between the two proteins that can modify their functions. Beyond these effects, some gene fusions may cause regulatory changes that alter when and where these genes act. For partial gene fusions, the shuffling of different active sites and binding domains have potential to result in new proteins with novel functions.

Recombinant technology

A recombinant fusion protein is a protein created through genetic engineering of a fusion gene. This typically involves removing the stop codon from a cDNA sequence coding for the first protein, then appending the cDNA sequence of the second protein in frame through ligation or overlap extension PCR. That DNA sequence will then be expressed by a cell as a single protein. The protein can be engineered to include the full sequence of both original proteins, or only a portion of either.

If the two entities are proteins, often linker (or "spacer") peptides are also added, which make it more likely that the proteins fold independently and behave as expected. Especially in the case where the linkers enable protein purification, linkers in protein or peptide fusions are sometimes engineered with cleavage sites for proteases or chemical agents that enable the liberation of the two separate proteins. This technique is often used for identification and purification of proteins, by fusing a GST protein, FLAG peptide, or a hexa-his peptide (6xHis-tag), which can be isolated using affinity chromatography with nickel or cobalt resins. Di- or multimeric chimeric proteins can be manufactured through genetic engineering by fusion to the original proteins of peptide domains that induce artificial protein di- or multimerization (e.g., streptavidin or leucine zippers). Fusion proteins can also be manufactured with toxins or antibodies attached to them in order to study disease development.

Chimeric protein drugs

Sketches of mouse (top-left), chimeric (top-right) and humanized (bottom-left) monoclonal antibodies. Human parts are shown in brown, and non-human parts in blue.

The purpose of creating fusion proteins in drug development is to impart properties from each of the "parent" proteins to the resulting chimeric protein. Several chimeric protein drugs are currently available for medical use.

Many chimeric protein drugs are monoclonal antibodies whose specificity for a target molecule was developed using mice and hence were initially "mouse" antibodies. As non-human proteins, mouse antibodies tend to evoke an immune reaction if administered to humans. The chimerization process involves engineering the replacement of segments of the antibody molecule that distinguish it from a human antibody. For example, human constant domains can be introduced, thereby eliminating most of the potentially immunogenic portions of the drug without altering its specificity for the intended therapeutic target. Antibody nomenclature indicates this type of modification by inserting -xi- into the non-proprietary name (e.g., abci-xi-mab). If parts of the variable domains are also replaced by human portions, humanized antibodies are obtained. Although not conceptually distinct from chimeras, this type is indicated using -zu- such as in dacli-zu-mab. See the list of monoclonal antibodies for more examples.

In addition to chimeric and humanized antibodies, there are other pharmaceutical purposes for the creation of chimeric constructs. Etanercept, for example, is a TNFα blocker created through the combination of a tumor necrosis factor receptor (TNFR) with the immunoglobulin G1 Fc segment. TNFR provides specificity for the drug target and the antibody Fc segment is believed to add stability and deliverability of the drug.

Natural occurrence

Naturally occurring fusion genes are most commonly created when a chromosomal translocation replaces the terminal exons of one gene with intact exons from a second gene. This creates a single gene that can be transcribed, spliced, and translated to produce a functional fusion protein. Many important cancer-promoting oncogenes are fusion genes produced in this way.

Examples include:

• Gag-onc fusion protein
• Bcr-abl fusion protein
• Tpr-met fusion protein

Antibodies are fusion proteins produced by VDJ recombination.

See also

• Genetic engineering
• Protein engineering

External links

Library resources about Fusion protein

Resources in your library Resources in other libraries

• Mutant Chimeric Proteins at the US National Library of Medicine Medical Subject Headings (MeSH)

UpToDate Contents

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• 1. 慢性骨髄性白血病の細胞生物学および分子生物学 cellular and molecular biology of chronic myeloid leukemia
• 2. 急性骨髄性白血病における細胞遺伝学 cytogenetics in acute myeloid leukemia
• 3. 未分化リンパ腫キナーゼ（ALK）融合癌遺伝子陽性非小細胞肺癌 anaplastic lymphoma kinase alk fusion oncogene positive non small cell lung cancer
• 4. アントラサイクリン系以外の癌化学療法剤の心毒性 cardiotoxicity of nonanthracycline cancer chemotherapy agents
• 5. 急性移植片対宿主病の治療 treatment of acute graft versus host disease

English Journal

• Nano-erythrocyte membrane-chaperoned 5-fluorouracil liposomes as biomimetic delivery platforms to target hepatocellular carcinoma cell lines.

• AlQahtani SA, Harisa GI, Badran MM, AlGhamdi KM, Kumar A, Salem-Bekhit MM, Ahmad SF, Alanazi FK.
• Artificial cells, nanomedicine, and biotechnology. 2019 Dec;47(1)989-996.
• Nano-erythrocyte coating has been developed as an interesting biomimetic platform to provide hybrid nano-carriers with innate functions to target liver cancer. This goal was achieved by coating nano-erythrocyte membranes (NEMs) onto 5-fluorouracil (5-FU)-loaded liposomes (LPs) to produce NEM-5-FU-LP
• PMID 30873877

• Enhancement of the effect of BCG vaccine against tuberculosis using DDA/TDB liposomes containing a fusion protein of HspX, PPE44, and EsxV.

• Mansury D, Ghazvini K, Amel Jamehdar S, Badiee A, Tafaghodi M, Nikpoor AR, Amini Y, Jaafari MR.
• Artificial cells, nanomedicine, and biotechnology. 2019 Dec;47(1)370-377.
• Tuberculosis has been a major health problem worldwide for years; therefore, it is important to develop and produce an effective vaccine against this disease. In this study, the immunogenicity of Mycobacterium tuberculosis fusion protein (FP) encapsulated in liposomes containing DDA/TDB was evaluate
• PMID 30691310

• The pilot-scale preparation of the SA-hGM-CSF bi-functional fusion protein.

• Li X, Zhou S, Wang Y, Lian H, Zuo A, Zhou K, Tong L, Zhou Z, Gao J.
• Bioengineered. 2019 12;10(1)108-120.
• The granulocyte-macrophage colony-stimulating factor (GM-CSF) can be used to induce a powerful immune response. Based on the specific binding of biotin and streptavidin, SA-hGM-CSF was anchored on the surface of biotinylated tumor cells, which could enhance the anti-tumor effect of tumor cell vaccin
• PMID 31017543

Japanese Journal

• Expression of the immunoreactive buckwheat major allergenic storage protein in Lactococcus lactis

• Shigemori Suguru,Yonekura Shinichi,Sato Takashi,Otani Hajime,Shimosato Takeshi
• APPLIED MICROBIOLOGY AND BIOTECHNOLOGY 97(8), 3603-3611, 2013-04-00
• … In this study, we successfully developed a modified lactic acid bacterial vector (pNSH) and a recombinant strain of Lactococcus lactis NZ9000 (NZ9000) that produced a major allergenic storage protein of buckwheat, Fagag1 (61.2 kDa, GenBank accession number AF152003), with or without a green fluorescent protein (GFP) tag. … GFP fluorescence allows for rapid, simple, and accurate measurement of target protein expression by microscopy or fluorimetry. …
• NAID 120005248205

• Evolutionary aspects of a unique internal mitochondrial targeting signal in nuclear-migrated rps19 of sugar beet (Beta vulgaris L.)

• Matsunaga Muneyuki,Takahashi Yoshiya,Yui-Kurino Rika,Mikami Tetsuo,Kubo Tomohiko
• GENE 517(1), 19-26, 2013-03-15
• … Here, we report the molecular cloning of a sugar beet gene for ribosomal protein S19 (Rps19; … Analyses of the intracellular localization of chimaeric GFP-fusion proteins that were transiently expressed in Welsh onion cells showed that Ntrps19-gfp was not localized in mitochondria. …
• NAID 120005228635

• 成長期の骨格性下顎前突症における下顎骨の過大な成長の予測 : 形態学的研究とゲノム解析を用いて

• 梶井 貴史
• 福岡歯科大学学会雑誌 38(3), 139-144, 2012-12-06
• … D1S0411i was located on chromosome 1p22.3 and was approximately 23 kb upstream of the SSX2IP (synovial sarcoma, X breakpoint 2 interacting protein) gene. … The fusion of morphological studies and genomic studies will develop custom-made orthodontic treatment in growing mandibular prognathism patients. …
• NAID 110009562432

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★リンクテーブル★

リンク元	「融合タンパク質」「キメラ蛋白質」「融合蛋白質」「融合タンパク」「F蛋白質」
拡張検索	「GFP fusion protein」「recombinant fusion protein」「Gag-Onc fusion protein」
関連記事	「fusion」

「融合タンパク質」

　　[★]

英

fusion protein

関

融合タンパク、融合蛋白、融合蛋白質

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融合蛋白 : 約 24,000 件
融合タンパク質 : 約 824,000 件
融合タンパク : 約 12,300 件
融合蛋白質 : 約 42,700 件

「キメラ蛋白質」

　　[★]

英

chimeric protein

同

融合蛋白質, fusion protein、ハイブリッド蛋白質 hybrid protein

関

キメラタンパク質、キメラタンパク、キメラ蛋白

「融合蛋白質」

　　[★]

英

fusion protein

同

融合タンパク質、融合タンパク、融合蛋白

関

F蛋白質、キメラ蛋白質

「融合タンパク」

　　[★]

英

fusion protein

関

融合タンパク質、融合蛋白、融合蛋白質

「F蛋白質」

　　[★]

英

F protein

同

融合蛋白質 fusion protein

「GFP fusion protein」

　　[★]

GFP融合タンパク質、GFP標識タンパク質

関

GFP-tagged、GFP-tagged protein

「recombinant fusion protein」

　　[★]

• 組換え融合タンパク質

「Gag-Onc fusion protein」

　　[★]

Gag-Onc融合タンパク質

「fusion」

　　[★]

• n.

• 溶解、溶融。融合、統合。(政治)連合。(原子力)核融合