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SARS Coronavirus is an enveloped virus containing three outer structural proteins, namely the membrane (M), envelope (E), and spike (S) proteins. Spike (S)-glycoprotein of the virus interacts with a cellular receptor and mediates membrane fusion to allow viral entry into susceptible target cells. Accordingly, S-protein plays an important role in virus infection cycle and is the primary target of neutralizing antibodies.

Cysteine Conjugate-Beta Lyase Cytoplasmic also known as CCBL1 is a member of the class-I pyridoxal-phosphate-dependent aminotransferase family. CCBL1 catalyzes the irreversible transamination of the L-tryptophan metabolite L-kynurenine to form kynurenic acid (KA) it also metabolizes the cysteine conjugates of certain halogenated alkenes and alkanes to form reactive metabolites. Furthermore, CCBL1 catalyzes the beta-elimination of S-conjugates and Se-conjugates of L-(seleno) cysteine, resulting in the cleavage of the C-S or C-Se bond.

Prolactin is a pituitary hormone involved in the stimulation of milk production, salt and water regulation, growth, development and reproduction. The initial step in its action is the binding to a specific membrane receptor (prolactin receptor) which belongs to the superfamily of class 1 cytokine receptors. The function of the prolactin receptor is mediated, at least in part, by two families of signaling molecules: Janus kinases and signal transducers and activators of transcription. Prolactin (PRL) is a hormone involved in a variety of important functions including ion transport and osmoregulation, stimulation of milk, protein synthesis as well as the regulation of numerous reproductive functions. PRL exerts its influence on different cell types through a signal transduction pathway which begins with the binding of the hormone to a transmembrane PRL receptor. Immunoreactive PRL receptor, a member of the cytokine receptor family, varies in size (short and long forms) with tissue source and species, from ~40 kDa to 100 kDa. The PRL receptor consists of at least three separate domains: an extracellular region with 5 cysteines which contains the prolactin binding site, a single transmembrane domain and a cytoplasmic region, the length of which appears to influence ligand binding and regulate cellular function.

Mouse Lungkine/CXCL15 (WECHE) belongs to the ELR motif-containing CXC chemokines. The mouse Lungkine gene has been mapped to chromosome 5. The cDNA of mouse Lungkine encodes a 166 amino acids (aa) protein with a 25 aa predicted signal peptide and a 141 aa mature protein with an exceptionally long C-terminal tail which extends beyond beyond the chemokine fold. Lungkine protein is secreted into bronchoalveolar space and is involved in lung-specific neutrophils trafficking. Furthermore, studies in Lungkine knockout mice propose that Lungkine is an imperative mediator of neutrophil migration from the lung parenchyma into the airspace. In addition, Lungkine is chemotactic for bone marrow progenitor cells and modulates hematopoietic cell differentiation. By Northern blot analysis and in-situ hybridization, Lungkine transcripts have only been specifically detected in the adult and fetal lung, and its expression is up-regulated under inflammatory conditions. There is a 35% aa sequence similarity between the mouse Lungkine and the human ENA-78 and a 31% similarity with the human IL-8.

LY86 is vital for effective CD180 cell surface expression and is vastly expressed in B-cells, tonsil and monocytes. LY86 collaborate with TLR4 and CD180 to facilitate the essential immune response to bacterial lipopolysaccharide (LPS) and cytokine production.

Shiga-like toxin (verotoxin) is a toxin produced by some strains of Escherichia coli. Shiga-like toxin is named for its similarity to the AB5-type Shiga toxin produced by the bacteria Shigella dysenteriae. There are two known types-SLT1 and SLT2. The Shiga-like toxin is linked with hemolytic-uremic syndrome. Shiga-like toxin requires highly specific receptors on the cells'' surface in order to attach and enter the cell. Species such as cattle, swine, and deer which do not carry these receptors may harbor toxigenic bacteria without any ill effect, dropping them in their feces, from where they may be distributed to humans. Shiga Like Toxin-1 Subunit B has nontoxic action, it is the functional region which binds to the receptor. The Shiga Like Toxin-1 Subunit B can be useful in vaccine study, antibody test and other functional research.

Lysophosphatidylcholine acyltransferase 1 (LPCAT1) is a part of the 1-acyl-sn-glycerol-3-phosphate acyltransferase family. LPCAT1 is a key enzyme for remodeling phospholipids, including phosphatidylcholine. LPCAT1 possesses both acyltransferase and acetyltransferase activities and also mediates the conversion of 1-acyl-sn-glycero-3-phosphocholine (LPC) into phosphatidylcholine (PC). LPCAT1 presents a clear preference for saturated fatty acyl-CoAs, and 1-myristoyl or 1-palmitoyl LPC as acyl donors and acceptors, respectively. LPCAT1 synthesizes phosphatidylcholine in pulmonary surfactant and therefore playing an important role in respiratory physiology.

ACY1 is a cytosolic, homodimeric, zinc-binding enzyme that catalyzes the hydrolysis of acylated L-amino acids to L-amino acids and acyl group, and has been postulated to take part in the catabolism and salvage of acylated amino acids. Defects in ACY1 are the source of aminoacylase-1 deficiency (ACY1D). ACY1D results in a metabolic disorder manifesting with encephalopathy, unspecific psychomotor delay, psychomotor delay with atrophy of the vermis and syringomyelia, marked muscular hypotonia or normal clinical features. Epileptic seizures are a frequent feature.

Beta-lactamase is a type of enzyme (EC 3.5.2.6) produced by some bacteria that is responsible for their resistance to beta-lactam antibiotics like penicillins, cephalosporins, cephamycins and carbapenems. These antibiotics have a common element in their molecular structure: a four-atom ring known as a beta-lactam. The lactamase enzyme breaks that ring open, deactivating the molecule's antibacterial properties.

The Proteinase K enzyme is a member of the Peptidase family S8. Proteinase K is a broad-spectrum serine protease. Proteinase K is capable of digesting hair (keratin), henceforth, the name "Proteinase K". Proteinase K is activated by calcium, the enzyme digests proteins especially after hydrophobic amino acids (aliphatic, aromatic and other hydrophobic amino acids). Proteinase K is frequently utilized in molecular biology to digest protein and remove contamination from preparations of nucleic acid. Addition of Proteinase K to nucleic acid preparations rapidly inactivates nucleases which may otherwise degrade the DNA or RNA during purification. Proteinase K is greatly fitting to this application as the enzyme is active in the presence of chemicals which denature proteins, such as SDS and urea, chelating agents such as EDTA, sulfhydryl reagents, as well as trypsin or chymotrypsin inhibitors. Proteinase K is utilized for the destruction of proteins in cell lysates (tissue, cell culture cells) and for the release of nucleic acids, given that it quite effectively inactivates DNases and RNases.

Thyroglobulin (TG) represents one of the main autoantigenic targets in autoimmune thyroid disease of humans. TG is a large globular dimeric glycoprotein with a total molecular weight of 660 kDa, which occupies a key precursor role in the biosynthesis of the thyroid hormones. Approximately 75% of the total protein content of the thyroid follicle consists of TG. The thyroid gland uses the Thyroglobulin in order to produce the thyroid hormones thyroxine (T4) and triiodothyronine (T3). Thyroglobulin is produced by the thyroid epithelial cells (thyrocytes) which form spherical follicles. Thyroglobulin is subsequently secreted and stored in the follicular lumen.
Patients with Hashimoto's thyroiditis or Graves' disease, frequently develop antibodies against Thyroglobulin. Tg-specific antibodies help in the diagnosis of the above diseases, however they also may be present in apparently healthy euthyroid individuals. Blood Thyroglobulin levels can be used as a tumor marker for certain kinds of thyroid cancer, and the may also be elevated in cases of Graves' disease.

The IL-6 receptor complex is composed of two membrane glycoproteins: the low affinity receptor and the signaltransducing component. The soluble form of IL6R is found in the urine of healthy adult humans and the serum of HIV positive individuals, as well as in the cell culture supernatants of stimulated PBMC’s. This soluble form of IL6R results from either proteolytic cleavage from the membrane, or an isoform derived splice variant.

Chemokine (C-C motif) ligand 11 (CCL11) is a small cytokine belonging to the CC chemokine family that is also known as eotaxin. CCL11 selectively recruits eosinophils by inducing their chemotaxis, and therefore, is implicated in allergic responses. The effects of CCL11 are mediated by its binding to a G-protein-linked receptor known as a chemokine receptor. Chemokine receptors for which CCL11 is a ligand include CCR2, CCR3 and CCR5. The gene for human CCL11 (scya11) is encoded on three exons and is located on chromosome 17.

Cathepsin-L also known as CTSL is a member of the peptidase C1 family. CTSL, is a dimer composed of disulfide-linked heavy and light chains, both formed from a single protein precursor. Furthermore, CTSL is a lysosomal cysteine proteinase which takes a main part in intracellular protein catabolism. CTSL substrates include collagen and elastin, as well as alpha-1 protease inhibitor, which is the most important controlling element of neutrophil elastase activity. CTSL has been implicated in a number of pathologic processes, including myofibril necrosis in myopathies and in myocardial ischemia, and in the renal tubular response to proteinuria. Multiple alternatively spliced transcript variants have been found for CTSL.

Recombinant Galectin-13 is an E. coli expressed peptide, this protein is one of human placenta specific galectins, like all galectin family, it contains a carbohydrate recognition domain (CRD) as well. Increased blood concentration was found highly asscoaited with preeclampsia and HELLP syndrome in pregnant women. The molecular weight of galectin-13 is 16kDa.

Leptin is a protein hormone. It is mainly produced in adipose cells that regulate energy homeostasis by restraining hunger. Leptin ties to nuclear receptors in the hypothalamus (arcuate nucleus). Similar to insulin resistance in type II diabetes, in obesity there is a decrease in the sensitivity towards leptin, ending in a failure to identify satiety, even in high levels of energy stores or leptin itself. Full-length cDNA encoding 2 leptin sequences (tLepA and tLepB) and 1 leptin receptor sequence (tLepR) exists in tilapia (Oreochromis niloticus). The full-length cDNA of tLepR is 3423 bp, encoding a protein of 1140 amino acid which contained all functionally important domains conserved among vertebrate leptin receptors. The cDNAs of tLepA and tLepB are 486 bp and 459 bp in length, encoding proteins of 161 aa and 152 aa, respectively. The three-dimensional structures of tLepA and tLepB demonstrates strong conservation of tertiary structure with that of human leptin comprised of 4 helixes.

Interleukin-1 ra is a member of the interleukin 1 cytokine family. This protein inhibits the activities of interleukin 1, alpha (IL1A) and interleukin 1, beta (IL1B), and modulates a variety of interleukin 1 related immune and inflammatory responses. This gene and five other closely related cytokine genes form a gene cluster spanning approximately 400 kb on chromosome 2. A polymorphism of this gene is reported to be associated with increased risk of osteoporotic fractures and gastric cancer. Four alternatively spliced transcript variants encoding distinct isoforms have been reported.

SARS or severe acute respiratory syndrome is a lethal kind of pneumonia generated by coronavirus. Coronaviruses are a family of viruses that causes a mild respiratory tract infection is a large type of creatures such as humans, pigs, cows, mice, cats etc. up to this day, the origin of the coronavirus is still unknown.

Cathepsins B, C, H, L, S, V, X/Z/P and 1 are cysteine proteases of the papain family. Cathepsin C is also known as DPPI (dipeptidyl-peptidase I). Cathepsin A is a serine carboxypeptidase and Cathepsin D and E are aspartic proteases. As lysosomal proteases, cathepsins play an important role in protein degradation. Because of their redistribution or increased levels in human and animal tumors, cathepsins may have a role in invasion and metastasis. Cathepsins are synthesized as inactive proenzymes and processed to become mature and active enzymes. Endogenous protein inhibitors, such as cystatins and some serpins, inhibit active enzymes.

L-Asparaginase is an enzyme that depletes L-Asparagine "an important nutrient for cancer cells" resulting in cancer/tumor cell starvation. L-asparaginase is an anti-tumor agent derived from E.coli.,which can inhibit the growth of malignant cells. It is used mainly for the induction of remission in acute lymphoblastic leukaemia. Because of the lymph node origin of malignant B cells in Multiple Myeloma, L-Asparagine is an essential amino acid for their cell metabolism, and, consequently, L-Asparaginase may be of value in managing the disease.
The rationale behind asparaginase is that it takes advantage of the fact that ALL cellsare unable to synthesize the non-essential amino acidasparaginewhereas normal cells are able to make their own asparagine. These leukemic cells depend on circulating asparagine. Asparaginase however catalyzes the conversion of L-asparagine to aspartic acidand ammonia. This deprives the leukemic cell of circulating asparagine.

Activins are homodimers or heterodimers of the different β subunit isoforms, part of the TGFβ family. Mature Activin A has two 116 amino acids residues βA subunits (βA-βA). Activin displays an extensive variety of biological activities, including mesoderm induction, neural cell differentiation, bone remodelling, haematopoiesis, and reproductive physiology. Activins takes part in the production and regulation of hormones such as FSH, LH, GnRH and ACTH. Cells that are identified to express Activin A include fibroblasts, endothelial cells, hepatocytes, vascular smooth muscle cells, macrophages, keratinocytes, osteoclasts, bone marrow monocytes, prostatic epithelium, neurons, chondrocytes, osteoblasts, Leydig cells, Sertoli cells, and ovarian granulosa cells.

E3 ubiquitin-protein ligase SIAH1 (SIAH1) belongs to the SIAH (seven in absentia homolog) family. SIAH1 is a tumor suppressor protein, which is expressed in intestinal epithelium and activated during apoptosis. SIAH1 is involved in ubiquitination and proteasome-mediated degradation of specific proteins. SIAH1 is comprised of an N-terminal RING-finger domain (required for proteolysis) and a cystein-rich C-terminal domain (which regulates oligomerization and SIAH binding to target proteins). SIAH1 causes indirect degradation of beta-catenin by way of creation of a complex with Siah-interacting protein (SIP), Skp1 and Ebi.

Nectin-1, also referred to as ED4, is a poliovirus receptor- related 1 protein is a part of the Nectin family. Nectin-1 endorses cell-cell contacts by forming homophilic or heterophilic trans-dimers. Heterophilic interactions among PVRL1/nectin-1 & PVRL4/nectin-4 and among PVRL1/nectin-1 & PVRL3/nectin-3 have been found. Nectin-1 acts as an entry receptor for herpes simplex virus & pseudorabies virus as well. Likewise, Neurite outgrowth-promoting activity has been shown by Nectin-1.

Calmodulin Like 5, also known as CALML5 is a part of the calmodulin family of calcium binding proteins. CALML5 undergoes a conformational change as a result of binding calcium. CALML5 is taking part in terminal differentiation of keratinocytes and encodes a calcium binding protein expressed in the epidermis.