Sample type Serum, Plasma, Cell Culture Supernatant, Other liquid samples
Components
Break apart microtiter test strips each coated single wells
8 x 12 (96 Total)
Lyophilized Standard
2 x vial
Biotin-labeled Antibody(Concentrated, 100X)
120 uL
HRP-Streptavidin Conjugate(Concentrated, 100X)
120 uL
Washing solution concentrate (25X)
30 mL
Sample Dilution buffer
20 mL
Antibody Dilution buffer
10 mL
Streptavidin Dilution buffer
10 mL
Stopping solution
10 mL
TMB Substrate (ready-to-use)
10 mL
Plate seals
3
Storage Store at 2-8°C.
target relevance
anti-Sotrovimab antibody Anti-drug antibodies (ADAs) generated in subjects following administration of Sotrovimab.
Sotrovimab Sotrovimab biologic drug binds Severe acute respiratory syndrome coronavirus 2 S Spike glycoprotein
Severe acute respiratory syndrome coronavirus 2 S Spike glycoprotein
Protein names Spike glycoprotein
Alternative names E2, Peplomer protein
Gene names S
Protein family Belongs to the betacoronaviruses spike protein family
Function Attaches the virion to the cell membrane by interacting with host receptor, initiating the infection. The major receptor is host ACE2 (PubMed:32142651, PubMed:32155444, PubMed:33607086). When S2/S2' has been cleaved, binding to the receptor triggers direct fusion at the cell membrane (PubMed:34561887). When S2/S2' has not been cleaved, binding to the receptor results in internalization of the virus by endocytosis using host TFRC and GRM2 and leading to fusion of the virion membrane with the host endosomal membrane (PubMed:32075877, PubMed:32221306, PubMed:34903715, PubMed:36779763). Alternatively, may use NRP1/NRP2 (PubMed:33082294, PubMed:33082293) and integrin as entry receptors (PubMed:35150743). The use of NRP1/NRP2 receptors may explain the tropism of the virus in human olfactory epithelial cells, which express these molecules at high levels but ACE2 at low levels (PubMed:33082293). Uses also ASGR1 as an alternative receptor in an ACE2-independent manner (PubMed:34837059). The stalk domain of S contains three hinges, giving the head unexpected orientational freedom (PubMed:32817270)
Structure Binds to host ACE2 (PubMed:32075877, PubMed:32132184, PubMed:32155444, PubMed:32221306, PubMed:32225175, PubMed:32225176, PubMed:33607086). RBD also interacts with the N-linked glycan on 'Asn-90' of ACE2 (PubMed:33607086). Cleavage of S generates a polybasic C-terminal sequence on S1 that binds to host Neuropilin-1 (NRP1) and Neuropilin-2 (NRP2) receptors (PubMed:33082293, PubMed:33082294). Interacts with host integrin alpha-5/beta-1 (ITGA5:ITGB1) and with ACE2 in complex with integrin alpha-5/beta-1 (ITGA5:ITGB1) (PubMed:33102950). May interact via cytoplasmic c-terminus with M protein (PubMed:33229438). May interact (via N-terminus) with host bilirubin and biliverdin, thereby preventing antibody binding to the SARS-CoV-2 spike NTD via an allosteric mechanism (PubMed:33888467). May interact with host LRRC15, thereby allowing attachment to host cells (PubMed:36735681)
Post-translational modification The cytoplasmic Cys-rich domain is palmitoylated. Palmitoylated spike proteins drive the formation of localized ordered cholesterol and sphingo-lipid-rich lipid nanodomains in the early Golgi, where viral budding occurs Specific enzymatic cleavages in vivo yield mature proteins. The precursor is processed into S1 and S2 by host furin or unknown proteases to yield the mature S1 and S2 proteins (PubMed:32155444, PubMed:32362314, PubMed:32703818, PubMed:34159616, PubMed:34561887). Processing between S2 and S2' occurs either by host CTSL in endosomes (PubMed:32221306, PubMed:33465165, PubMed:34159616), or by host TMPRSS2 at the cell surface (PubMed:32142651). Both cleavages are necessary for the protein to be fusion competent (PubMed:32703818, PubMed:34159616, PubMed:34561887). Cell surface activation allows the virus to enter the cell despite inhibition of the endosomal pathway by hydroxychloroquine (PubMed:33465165). The polybasic furin cleavage site is absent in SARS-CoV S (PubMed:32155444, PubMed:32362314, PubMed:33465165). It increases the dependence on TMPRSS2 expression by SARS-CoV-2 (PubMed:33465165). D614G substitution would enhance furin cleavage at the S1/S2 junction (PubMed:33417835) Highly decorated by heterogeneous N-linked glycans protruding from the trimer surface (PubMed:32075877, PubMed:32155444, PubMed:32929138). Highly glycosylated by host both on S1 and S2 subunits, occluding many regions across the surface of the protein (PubMed:32363391, PubMed:32366695, PubMed:32929138). Approximately 40% of the protein surface is shielded from antibody recognition by glycans, with the notable exception of the ACE2 receptor binding domain (PubMed:32929138) O-glycosylated by host GALNT1 at the end of S1. This could reduce the efficiency of S1/S2 cleavage
Keywords 3D-structure, Coiled coil, Disulfide bond, Fusion of virus membrane with host endosomal membrane, Fusion of virus membrane with host membrane, Glycoprotein, Host cell membrane, Host membrane, Host-virus interaction, Inhibition of host innate immune response by virus, Inhibition of host tetherin by virus, Lipoprotein, Membrane, Palmitate, Reference proteome, Signal, Superantigen, Transmembrane, Transmembrane helix, Viral attachment to host cell, Viral envelope protein, Viral immunoevasion, Viral penetration into host cytoplasm, Virion, Virulence, Virus entry into host cell
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Published literature highly relevant to the biological target of this product and referencing this antibody or clone are retrieved from the PubMed database provided by the United States National Library of Medicine at the National Institutes of Health.
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