SARS S2 [His] (DAG1862)

SARS S2 [His], recombinant protein from E. coli

Product Overview
S2 (SARS) (P59594) partial recombinant protein with GST tag expressed inEscherichia coli .
Nature
Recombinant
Tag/Conjugate
His
Procedure
None
Purity
Ion exchange column and HPLC reverse phase column
Format
Lyophilized
Buffer
Lyophilized from 50 mM Tris-HCl, 60 mM NaCl (50% glycerol)
Preservative
None
Storage
2-8°C short term, -20°C long term
Introduction
Severe acute respiratory syndrome is a viral respiratory disease in humans which is caused by the SARS coronavirus (SARS-CoV). Between November 2002 and July 2003, an outbreak of SARS in Hong Kong nearly became a pandemic, with 8, 422 cases and 916 deaths worldwide (10.9% fatality) according to the World Health Organization. Within weeks, SARS spread from Hong Kong to infect individuals in 37 countries in early 2003.[

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References


Attenuated SARS-CoV-2 variants with deletions at the S1/S2 junction

EMERGING MICROBES & INFECTIONS

Authors: Lau, Siu-Ying; Wang, Pui; Mok, Bobo Wing-Yee; Zhang, Anna Jinxia; Chu, Hin; Lee, Andrew Chak-Yiu; Deng, Shaofeng; Chen, Pin; Chan, Kwok-Hung; Song, Wenjun; Chen, Zhiwei; To, Kelvin Kai-Wang; Chan, Jasper Fuk-Woo; Yuen, Kwok-Yung; Chen, Honglin

The emergence of SARS-CoV-2 has led to the current global coronavirus pandemic and more than one million infections since December 2019. The exact origin of SARS-CoV-2 remains elusive, but the presence of a distinct motif in the S1/S2 junction region suggests the possible acquisition of cleavage site(s) in the spike protein that promoted cross-species transmission. Through plaque purification of Vero-E6 cultured SARS-CoV-2, we found a series of variants which contain 15-30-bp deletions (Del-mut) or point mutations respectively at the S1/S2 junction. Examination of the original clinical specimen from which the isolate was derived, and 26 additional SARS-CoV-2 positive clinical specimens, failed to detect these variants. Infection of hamsters shows that one of the variants (Del-mut-1) which carries deletion of 10 amino acids (30bp) does not cause the body weight loss or more severe pathological changes in the lungs that is associated with wild type virus infection. We suggest that the unique cleavage motif promoting SARS-CoV-2 infection in humans may be under strong selective pressure, given that replication in permissive Vero-E6 cells leads to the loss of this adaptive function. It would be important to screen the prevalence of these variants in asymptomatic infected cases. The potential of the Del-mut variants as an attenuated vaccine or laboratory tool should be evaluated.

Efficient production of recombinant SARS-CoV-2 spike protein using the baculovirus-silkworm system

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS

Authors: Fujita, Ryosuke; Hino, Masato; Ebihara, Takeru; Nagasato, Takumi; Masuda, Akitsu; Lee, Jae Man; Fujii, Tsuguru; Mon, Hiroaki; Kakino, Kohei; Nagai, Ryo; Tanaka, Miyu; Tonooka, Yoshino; Moriyama, Takato; Kusakabe, Takahiro

In the case of a new viral disease outbreak, an immediate development of virus detection kits and vaccines is required. For COVID-19, we established a rapid production procedure for SARS-CoV-2 spike protein (S protein) by using the baculovirus-silkworm expression system. The baculovirus vector-derived S proteins were successfully secreted to silkworm serum, whereas those formed insoluble structure in the larval fat body and the pupal cells. The ectodomain of S protein with the native sequence was cleaved by the host furin-protease, resulting in less recombinant protein production. The S protein modified in furin protease-target site was efficiently secreted to silkworm serum and was purified as oligomers, which showed immunoreactivity for anti-SARS-CoV-2 S2 antibody. By using the direct transfection of recombinant bacmid to silkworms, we achieved the efficient production of SARS-CoV-2 S protein as fetal bovine serum (FBS)-free system. The resultant purified S protein would be useful tools for the development of immunodetection kits, antigen for immunization for immunoglobulin production, and vaccines. (C) 2020 Published by Elsevier Inc.

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