escherichia

Integrase is necessary for integration of the phage into the host genome by site-specific recombination. In conjunction with excisionase, integrase is also necessary for excision of the prophage from the host genome. Integrase Protein, Escherichia phage lambda, Recombinant (His) is expressed in E. coli expression system with N-6xHis tag. The predicted molecular weight is 46.3 kDa and the accession number is P03700.

Stabilizes the expansion of the capsid head shell after genome packaging. The packaging of viral genome in the procapsid triggers a dramatic reconfiguration of the capsid shell, expanding from roughly 50nm to 60nm while the capsid thickness decreases. 415 capsid decoration protein molecules cooperatively bind the expanded capsid, thereby stabilizing the mature capsid shell. Capsid decoration Protein, Escherichia phage lambda, Recombinant (GST) is expressed in E. coli expression system with N-GST tag. The predicted molecular weight is 32.5 kDa and the accession number is P03712.

Capsid protein self-assembles to form an icosahedral capsid with a T=3 symmetry, about 26 nm in diameter, and consisting of 89 capsid proteins dimers (178 capsid proteins). Involved in viral genome encapsidation through the interaction between a capsid protein dimer and the multiple packaging signals present in the RNA genome. The capsid contains also 1 copy of the A2 maturation protein.; Acts as a translational repressor of viral replicase synthesis late in infection. This latter function is the result of capsid protein interaction with an RNA hairpin which contains the replicase ribosome-binding site.

Filamentous M13 phage extrude from infected Escherichia coli with a tip structure composed of gp7 and gp9. This tip structure is extended by the assembly of the filament composed of the major coat protein gp8. gp7, gp8 and gp9 could also be used for phage display and these phage particles should bind to two different or more surfaces when the modified coat proteins are combined. The gp9 at the phage tip is suitable for the phage display technology.

LTB (Lymphotoxin Beta) is a Protein Coding gene. 2 alternatively spliced human isoforms have been reported. Lymphotoxin beta is a type II membrane protein of the TNF family. It anchors lymphotoxin-alpha to the cell surface through heterotrimer formation. Heat-labile enterotoxin B subunit (LTB) of enterotoxigenic Escherichia coli (ETEC) is both a strong mucosal adjuvant and immunogen. It is a subunit vaccine candidate to be used against ETEC-induced diarrhea. It has already been expressed in several bacterial and plant systems.LTB provokes a systemic immune response and exerts adjuvant effects on mucosal immune responses to unrelated antigens. Diseases associated with LTB include Synovitis and Myasthenic Syndrome, Congenital, 2C, Associated With Acetylcholine Receptor Deficiency.

Aminopeptidase P (APP) is a hydrolase specific for N-terminal imido bonds, which are common to several collagen degradation products, neuropeptides, vasoactive peptides, and cytokines. A membrane-bound and soluble form of this enzyme (XPNPEP2) have been identified as products of two separate genes. XPNPEP2, the X-linked gene that encodes membranous aminopeptidase P (APP), has been reported to associate with APP activity. The membrane aminopeptidase P (XPNPEP2) is largely limited in distribution to endothelia and brush border epithelia. APP and XPNPEP2 contain homologous blocks of sequence common to members of the pita bread-fold protein family, of which Escherichia coli methionine aminopeptidase is the prototype. The C-2399A variant in XPNPEP2 is associated with reduced APP activity and a higher incidence of AE-ACEi. XPNPEP2 mRNA was detected in fibroblasts that carry the translocation, suggesting that this gene at least partially escapes X inactivation. XPNPEP2 is a candidate gene for premature ovarian failure (POF).

Escherichia coli contains two major aconitases (Acns), AcnA and AcnB. They are distantly related monomeric Fe-S proteins that contain different arrangements of four structural domains. acnA is specifically subject to SoxRS-mediated activation, whereas acnB encodes the major aconitase that is synthesized earlier in the growth cycle than AcnA. It is concluded that AcnB is the major citric acid cycle enzyme. Aconitate hydratase 2 (acnB) catalyzes the isomerization of citrate to isocitrate via cis-aconitate as well as the dehydration of 2-methylisocitrate to cis-2-methylaconitate, thus it functions as the major citric-acid-cycle enzyme during exponential growth. Escherichia coli acnB serves as either an enzymic catalyst or a mRNA-binding post-transcriptional regulator, depending on the status of its iron sulfur cluster. AcnB represents a large, distinct group of Gram-negative bacterial aconitases that have an altered domain organization relative to mitochondrial aconitase and other aconitases.

E. Coli STX2B is a subunit of Stx2. Stx2, together with Stx1, formed a family of related toxins which are known as shiga toxins. Shiga toxins are mainly produced by the bacteria S. dysenteriae and the Shigatoxigenic group of Escherichia coli, which includes serotypes O157:H7, O104:H4, and other enterohemorrhagic E. coli (EHEC). A total of 3222 outbreak cases (including 39 deaths) have been reported in northern Germany in May through June 2011. The outbreak strain was typed as an enteroaggregative Shiga-toxin–producing E. coli O104:H4, producing extended-spectrum beta-lactamase. The toxin has two subunits—A and B. E. Coli STX2B is the B subunit. It is a pentamer that binds to specific glycolipids on the host cell, specifically globotriaosylceramide. Following this, the A subunit is internalised and cleaved into two parts. Stx2 has been found to be approximately 400 times more toxic (as quantified by LD50 in mice) than Stx-1. The Stx1 and Stx2 B subunits form a pentameric structure that binds to globotriaosylceramide receptors on eukaryotic cells and promotes endocytosis.

Decay Accelerating Factor (or CD55) is a major regulator of the alternative and classical pathways of complement activation and is expressed on all serum-exposed cells. It is commonly hijacked by invading pathogens, including many enteroviruses and uropathogenic Escherichia coli, to promote cellular attachment prior to infection.