Poliovirus receptor, Nectin-like protein 5, NECL-5, CD155, PVR, PVS.
Greater than 90.0% as determined by SDS-PAGE.
PVR Human Recombinant produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 331 amino acids (21-343 a.a.) and having a molecular mass of 36.1kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa). PVR is expressed with an 8 amino acids His tag at C-Terminus and purified by proprietary chromatographic techniques.
Poliovirus receptor, Nectin-like protein 5, NECL-5, CD155, PVR, PVS.
WPPPGTGDVV VQAPTQVPGF LGDSVTLPCY LQVPNMEVTH VSQLTWARHG ESGSMAVFHQ TQGPSYSESK RLEFVAARLG AELRNASLRM FGLRVEDEGN YTCLFVTFPQ GSRSVDIWLR VLAKPQNTAE VQKVQLTGEP VPMARCVSTG GRPPAQITWH SDLGGMPNTS QVPGFLSGTV TVTSLWILVP SSQVDGKNVT CKVEHESFEK PQLLTVNLTV YYPPEVSISG YDNNWYLGQN EATLTCDARS NPEPTGYNWS TTMGPLPPFA VAQGAQLLIR PVDKPINTTL ICNVTNALGA RQAELTVQVK EGPPSEHSGM SRNLEHHHHH H
The Poliovirus Receptor (PVR), also known as CD155, is a type I transmembrane glycoprotein that belongs to the immunoglobulin superfamily. It plays a crucial role in various cellular processes, including cell adhesion, migration, and immune response regulation. The receptor is particularly notable for its role in poliovirus attachment and entry into host cells, making it a significant focus of virology and immunology research .
PVR is encoded by the PVR gene located on chromosome 19q13.31 in humans . The protein consists of an extracellular domain that mediates cell attachment to the extracellular matrix molecule vitronectin, a transmembrane domain, and an intracellular domain that interacts with the dynein light chain Tctex-1/DYNLT1 . This structure allows PVR to participate in the formation of intercellular adherens junctions between epithelial cells .
The primary function of PVR is to serve as a cellular receptor for poliovirus. The virus binds to the extracellular domain of PVR, facilitating its entry into the host cell and initiating the viral replication process . This interaction is the first step in poliovirus infection and is critical for the virus’s ability to infect human cells.
Beyond its role in viral entry, PVR has significant immunological functions. It is involved in the regulation of immune responses, particularly in the context of natural killer (NK) cell-mediated cytotoxicity. PVR interacts with activating receptors such as DNAM-1 and inhibitory receptors like TIGIT and CD96 on immune cells, influencing their activation and inhibition . This balance is crucial for maintaining normal immune function and preventing immune escape by tumor cells .
Recent research has highlighted the potential of targeting PVR in anti-tumor therapies. PVR is overexpressed in several human malignancies, where it promotes tumor cell invasion, migration, and proliferation . Strategies targeting PVR and its interactions with immune cell receptors are being explored to enhance anti-tumor responses and improve the efficacy of immunotherapies .
Human recombinant PVR is produced using recombinant DNA technology, which involves inserting the PVR gene into an expression system to produce the protein in vitro. This recombinant form is used in various research applications, including studies on poliovirus infection mechanisms, immune response regulation, and the development of therapeutic interventions.