Anti-HCoV HKU1 spike glycoprotein monoclonal antibody (CABT-RM316)

Rabbit anti-HCoV HKU1 spike glycoprotein monoclonal antibody for ELISA

Specifications


Host Species
Rabbit
Antibody Isotype
IgG
Clone
139
Species Reactivity
HCoV
Immunogen
Recombinant Human coronavirus spike glycoprotein protein
Conjugate
unconjugated

Applications


Application Notes
ELISA: 1:5000-1:10000
*Suggested working dilutions are given as a guide only. It is recommended that the user titrates the product for use in their own experiment using appropriate negative and positive controls.

Target


Alternative Names
HCoV spike glycoprotein;HCoV;Coronavirus;Human Coronavirus;HCoV S glycoprotein;HCoV S protein

Citations


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References


Crystal structure of the post-fusion core of the Human coronavirus 229E spike protein at 1.86 angstrom resolution

ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY

Authors: Yan, Lei; Meng, Bing; Xiang, Jiangchao; Wilson, Ian A.; Yang, Bei

Human coronavirus 229E (HCoV-229E) usually causes mild upper respiratory infections in heathy adults, but may lead to severe complications or mortality in individuals with weakened immune systems. Virus entry of HCoV-229E is mediated by its spike (S) protein, where the S1 domain facilitates attachment to host cells and the S2 domain is involved in subsequent fusion of the virus and host membranes. During the fusion process, two heptad repeats, HR1 and HR2, in the S2 domain assemble into a six-helix membrane-fusion structure termed the fusion core. Here, the complete fusion-core structure of HCoV-229E has been determined at 1.86 angstrom resolution, representing the most complete post-fusion conformation thus far among published human alphacoronavirus (-HCoV) fusion-core structures. The overall structure of the HCoV-229E fusion core is similar to those of SARS, MERS and HCoV-NL63, but the packing of its 3HR1 core differs from those of SARS and MERS in that it contains more noncanonical `x' and `da' layers. Side-by-side electrostatic surface comparisons reveal that the electrostatic surface potentials are opposite in -HCoVs and -HCoVs at certain positions and that the HCoV-229E surface also appears to be the most hydrophobic among the various HCoVs. In addition to the highly conserved hydrophobic interactions between HR1 and HR2, some polar and electrostatic interactions are also well preserved across different HCoVs. This study adds to the structural profiling of HCoVs to aid in the structure-based design of pan-coronavirus small molecules or peptides to inhibit viral fusion.

Cleavage of a Neuroinvasive Human Respiratory Virus Spike Glycoprotein by Proprotein Convertases Modulates Neurovirulence and Virus Spread within the Central Nervous System

PLOS PATHOGENS

Authors: Le Coupanec, Alain; Desforges, Marc; Meessen-Pinard, Mathieu; Dube, Mathieu; Day, Robert; Seidah, Nabil G.; Talbot, Pierre J.

Human coronaviruses (HCoV) are respiratory pathogens that may be associated with the development of neurological diseases, in view of their neuroinvasive and neurotropic properties. The viral spike (S) glycoprotein is a major virulence factor for several coronavirus species, including the OC43 strain of HCoV (HCoV-OC43). In an attempt to study the role of this protein in virus spread within the central nervous system (CNS) and neurovirulence, as well as to identify amino acid residues important for such functions, we compared the sequence of the S gene found in the laboratory reference strain HCoV-OC43 ATCC VR-759 to S sequences of viruses detected in clinical isolates from the human respiratory tract. We identified one predominant mutation at amino acid 758 (from RRSR down arrow(G) under bar 758 to RRSR down arrow(R) under bar 758), which introduces a putative furin-like cleavage (down arrow) site. Using a molecular cDNA infectious clone to generate a corresponding recombinant virus, we show for the first time that such point mutation in the HCoV-OC43 S glycoprotein creates a functional cleavage site between the S1 and S2 portions of the S protein. While the corresponding recombinant virus retained its neuroinvasive properties, this mutation led to decreased neurovirulence while potentially modifying the mode of virus spread, likely leading to a limited dissemination within the CNS. Taken together, these results are consistent with the adaptation of HCoV-OC43 to the CNS environment, resulting from the selection of quasi-species harboring mutations that lead to amino acid changes in viral genes, like the S gene in HCoV-OC43, which may contribute to a more efficient establishment of a less pathogenic but persistent CNS infection. This adaptative mechanism could potentially be associated with human encephalitis or other neurological degenerative pathologies.

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