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The scientific community is working at full speed to investigate and fight severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2). Miltenyi Biotec stands committed to assisting those researchers in getting to the bottom of COVID-19.
SARS-CoV-2 antigens offer researchers the possibility to investigate virus-specific immune responses, including antigen-specific B cells and antibodies.
Overview of our antigens for SARS-CoV-2 research. All antigens are available with or without biotinylation:
|Protein||Sequence part||Production specification|
|ACE2||Full length (with CLD)||Recombinant protein|
|Truncated (w/o CLD)||Recombinant protein|
|Spike protein||Receptor binding domain (RBD)||Recombinant protein|
|Nucleoprotein||Full length||Recombinant protein|
|Envelope protein||C-Terminus||Synthetic polypeptide|
|Helical segment 2 (H2)||Synthetic polypeptide|
Detection of patient-derived antibodies against SARS-CoV-2 antigens via a bead-based immunoassay
Biotinylated recombinant proteins coupled to streptavidin-coated PMMA beads can be applied to detect SARS-CoV-2–specific antibodies in plasmapheresis samples of COVID-19+ patients.
Cell-based assay to analyze the binding of RBD to native ACE2
The combination of recombinant RBD and ACE2-expressing cells can be used to mimic the binding of SARS-CoV-2 to its host cells in vitro. Such binding assays can be applied to study inhibitory/neutralizing effects of components or antibodies.
Angiotensin-converting enzyme 2 (ACE2, also known as ACEH) is a transmembrane protein, which acts as receptor for SARS-CoV, SARS-CoV-2, and other coronaviruses. The large extracellular peptidase domain of ACE2 is known to interact with the spike protein of coronaviruses. The small C-terminal collectrin-like domain (CLD) has recently been described to mediate homo-dimerization of ACE2.
We offer recombinant human ACE2 produced in HEK cells including C-terminal CLD or insect cell–derived ACE2 lacking CLD. The potential influence of the CLD domain is indicated by the exemplary analysis below.
The surface or spike (S) glycoprotein plays a critical role in coronavirus infection as it is crucial for recognition and fusion of the virus with the host cell membrane. Two different functional domains of the S protein are responsible for these individual processes: The S1 domain contains the receptor binding domain, which binds to the host cell receptor ACE2, whereas membrane fusion is mediated via the S2 domain. Furthermore, cleavage at the boundary of the S1 and S2 domains (aa residues 685 and 686) via cellular proteases primes the protein for entry into the host cell. Upon fusion of the viral envelope to the host cell membrane, the viral genome enters the host cell and viral replication starts.
The receptor binding domain (RBD) locates C-terminally within the S1 subunit of the S protein. The S protein forms a homotrimeric structure on the surface of the SARS-CoV-2 virus. Recent studies have shown that the predominant activated form of the protein S trimer displays one RBD rotated up into an ACE2-accessible state. Binding of RBD to ACE2 is a major contributor for interaction of protein S with its target receptor.
The SARS-CoV-2 nucleoprotein (also known as nucleocapsid protein or protein N) is a key structural protein of the SARS-CoV-2 virus. The N-terminal RNA-binding domain (NTD) associates with the viral genome of SARS-CoV-2. An intrinsically disordered stretch connects the NTD domain with the C-terminal dimerization domain (CTD). A major function of protein N is the packaging of the viral genome into helical nucleocapsid structures. Additionally, it is involved in virus transcription and interacts with the viral membrane during virion assembly.
The envelope protein (also known as envelope small membrane protein) is localized on the surface of the virus and represents one of the most relevant structural proteins of SARS-CoV-2. It acts as a viroporin and is involved in virus morphogenesis, assembly, and pathogenesis. Based on previous structural studies of highly similar envelope proteins from other coronaviruses and homology studies, it is assumed that the envelope protein forms a pentameric structure when integrated into the membrane of SARS-CoV-2.
We offer synthesized polypeptides for three parts of the envelope protein: C- terminus, N-terminus, and helical segment 2 (H2).
If you have further questions or are interested in our proteins for SARS-CoV-2 research, please specify your question or request in the contact form and we will come back to you:
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