Monkeypox Virus (MPXV), the virus that causes monkeypox infection in both humans and animals, is a double-stranded DNA virus that has had a recent global outbreak in 2022 . MPXV belongs to the Poxviridae family of viruses . It consists of several key subunits including a surface membrane fusion protein (A29L, ~14 kDa), two separate envelope proteins (A30L ~14 kDa and H3L ~32kDa), an envelope glycoprotein, A35R ~15 kDa), a receptor glycoprotein that mimics IFN-alpha/beta (B16, ~37 kDa), a palmitoylated EEV membrane glycoprotein (C19L, ~35 kDa), a secreted IL-18 binding protein (D6L, ~14 kDa), a cell surface-binding protein (E8L, ~32 kDa), a telomere binding protein (I1L, ~36kDa), and a subunit required for DNA packaging (L1R, 18 kDa) .
Monkeypox Virus (MPXV), the virus that causes monkeypox infection in both humans and animals, is a double-stranded DNA virus that has had a recent global outbreak in 2022. MPXV belongs to the Poxviridae family of viruses. It consists of several key subunits including a surface membrane fusion protein (A29L, ~14 kDa), two separate envelope proteins (A30L,~14 kDa and H3L, ~32kDa), an envelope glycoprotein (A35R ~15 kDa), a receptor glycoprotein that mimics IFN-alpha/beta (B16, ~37kDa), a palmitoylated EEV membrane glycoprotein (C19L, ~35 kDa), a secreted IL-18 binding protein (D6L, ~14kDa), a cell surface-binding protein (E8L, ~32 kDa), a telomere binding protein (I1L, ~36kDa), and a subunit required for DNA packaging (L1R, 18 kDa).
Forms a non-covalent specific complex with biotin. Monomeric streptavidin has unique structural and functional properties that can lead to development of new applications based on the well-known protein–ligand interaction. For example, it allows detection of biotinylated ligands while avoiding target aggregation caused by multivalent binding. Since clustering of biologically active molecules often results in functional changes, monomeric streptavidin can facilitate imaging and tracking studies in live cells by ensuring monovalent biotin binding.
YWHAE, also known as 14-3-3 epsilon, mediate signal transduction by binding to phosphoserine-containing proteins. 14-3-3 epsilon / YWHAE is a member of the 14-3-3 proteins family. 14-3-3 proteins are a group of highly conserved proteins that are involved in many vital cellular processes such as metabolism, protein trafficking, signal transduction, apoptosis and cell cycle regulation. 14-3-3 proteins are mainly localized in the synapses and neuronal cytoplasm, and seven isoforms have been identified in mammals. This family of proteins was initially identified as adaptor proteins which bind to phosphoserine-containing motifs. Binding motifs and potential functions of 14-3-3 proteins are now recognized to have a wide range of functional relevance. 14-3-3 epsilon / YWHAE is found in both plants and mammals, and this protein is 100% identical to the mouse ortholog. YWHAE interacts with CDC25 phosphatases, RAF1 and IRS1 proteins, suggesting its role in diverse biochemical activities related to signal transduction, such as cell division and regulation of insulin sensitivity. It has also been implicated in the pathogenesis of small cell lung cancer. 14-3-3 epsilon / YWHAE is implicated in the regulation of a large spectrum of both general and specialized signaling pathways. 14-3-3 epsilon / YWHAE Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. This Binding generally results in the modulation of the activity of the binding partner.
14-3-3 protein sigma (YWHAS), also known as stratifin (SFN) and epithelial cell marker protein 1, is a member of the14-3-3 proteins which are a family of conserved regulatory molecules expressed in all eukaryotic cells. The name 14-3-3 refers to the particular elution and migration pattern of these proteins on DEAE-cellulose chromatography and starch-gel electrophoresis. The 14-3-3 proteins eluted in the 14th fraction of bovine brain homogenate and were found on positions 3.3 of subsequent electrophoresis. There are seven genes that encode 14-3-3s in most mammals. 14-3-3 proteins have been identified as adapter proteins implicated in the regulation of a large spectrum of both general and specialized signaling pathway. More than 100 signaling proteins have been reported as 14-3-3 ligands including kinases, phosphatases, and transmembrane receptors, and the binding generally results in the modulation of the activity of the binding partner. YWHAE exists as a homodimer and present mainly in tissues enriched in stratified squamous keratinising epithelium. YWHAS has been repoted to interact with KRT17 and GAB2, and may regulate protein synthesis and epithelial cell growth by stimulating Akt/mTOR pathway upon binding to KRT17. Additionally, YWHAS (SFN) may also act as a p53-regulated inhibitor of G2/M progression.
Natural killer cell receptor 2B4 (2B4/CD244)is a 66 kDa type I transmembrane glycoprotein in the SLAM subgroup of the CD2 protein family. SLAM family proteins have an extracellular domain (ECD) with two or four Ig-like domains and at least two cytoplasmic immunoreceptor tyrosine-based switch motifs (ITSMs). 2B4 interacts with CD48, while other SLAM family proteins interact in a homophilic manner. The mouse 2B4 cDNA encodes a 397 amino acid (aa) precursor that includes a 19 aa signal sequence, a 207 aa ECD with one Ig-like V-type and one C2-type Ig-like domain, a 21 aa transmembrane segment, and a 150 aa cytoplasmic domain with four ITSMs. Within the ECD, mouse 2B4 shares 46% and 68% aa sequence identity with human and rat 2B4, respectively. 2B4/CD48 signaling cooperates with other receptor systems to either promote or inhibit NK and CD8+ T cell activation. The inhibitory activities are distinct from those of MHC I restricted inhibitory NK cell receptors. Ligation of 2B4 with antibodies or CD48 constructs can directly trigger inhibitory signaling or disrupt an inhibitory interaction, leading to cellular activation. 2B4 can also induce signaling through CD48.
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