Anti-MERS-CoV Spike Protein polyclonal antibody (CABT-B1957)

Rabbit Anti-MERS-CoV Spike Protein (aa 1-1297) polyclonal antibody for WB, ELISA, IHC, IF, IP

Specifications


Host Species
Rabbit
Antibody Isotype
IgG
Species Reactivity
MERS-CoV
Immunogen
Recombinant MERS-CoV (NCoV / Novel coronavirus) Spike Protein (ECD, aa 1-1297)
Conjugate
Unconjugated

Applications


Application Notes
WB: 0.5-1 μg/mL
ELISA: 0.1-0.2 μg/mL
*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
Novel coronavirus Spike Protein

Citations


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References


Host cell proteases: Critical determinants of coronavirus tropism and pathogenesis

VIRUS RESEARCH

Authors: Millet, Jean Kaoru; Whittaker, Gary R.

Coronaviruses are a large group of enveloped, single-stranded positive-sense RNA viruses that infect a wide range of avian and mammalian species, including humans. The emergence of deadly human coronaviruses, severe acute respiratory syndrome coronavirus (SARS-CoV), and Middle East respiratory syndrome coronavirus (MERS-CoV) have bolstered research in these viral and often zoonotic pathogens. While coronavirus cell and tissue tropism, host range, and pathogenesis are initially controlled by interactions between the spike envelope glycoprotein and host cell receptor, it is becoming increasingly apparent that proteolytic activation of spike by host cell proteases also plays a critical role. Coronavirus spike proteins are the main determinant of entry as they possess both receptor binding and fusion functions. Whereas binding to the host cell receptor is an essential first step in establishing infection, the proteolytic activation step is often critical for the fusion function of spike, as it allows for controlled release of the fusion peptide into target cellular membranes. Coronaviruses have evolved multiple strategies for proteolytic activation of spike, and a large number of host proteases have been shown to proteolytically process the spike protein. These include, but are not limited to, endosomal cathepsins, cell surface transmembrane protease/serine (TMPRSS) proteases, furin, and trypsin. This review focuses on the diversity of strategies coronaviruses have evolved to proteolytically activate their fusion protein during spike protein biosynthesis and the critical entry step of their life cycle, and highlights important findings on how proteolytic activation of coronavirus spike influences tissue and cell tropism, host range and pathogenicity. (C) 2014 Elsevier B.V. All rights reserved.

A camel-derived MERS-CoV with a variant spike protein cleavage site and distinct fusion activation properties

EMERGING MICROBES & INFECTIONS

Authors: Millet, Jean Kaoru; Goldstein, Monty E.; Labitt, Rachael N.; Hsu, Hung-Lun; Daniel, Susan; Whittaker, Gary R.

Middle East respiratory syndrome coronavirus (MERS-CoV) continues to circulate in both humans and camels, and the origin and evolution of the virus remain unclear. Here we characterize the spike protein of a camel-derived MERS-CoV (NRCE-HKU205) identified in 2013, early in the MERS outbreak. NRCE-HKU205 spike protein has a variant cleavage motif with regard to the S2' fusion activation site-notably, a novel substitution of isoleucine for the otherwise invariant serine at the critical P1' cleavage site position. The substitutions resulted in a loss of furin-mediated cleavage, as shown by fluorogenic peptide cleavage and western blot assays. Cell-cell fusion and pseudotyped virus infectivity assays demonstrated that the S2' substitutions decreased spike-mediated fusion and viral entry. However, cathepsin and trypsin-like protease activation were retained, albeit with much reduced efficiency compared with the prototypical EMC/2012 human strain. We show that NRCE-HKU205 has more limited fusion activation properties possibly resulting in more restricted viral tropism and may represent an intermediate in the complex pattern of MERS-CoV ecology and evolution.

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