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Spike (S) glycoprotein (sometimes also called spike protein, [2] formerly known as E2 [3]) is the largest of the four major structural proteins found in coronaviruses. [4] The spike protein assembles into trimers that form large structures, called spikes or peplomers, [3] that project from the surface of the virion.
For this reason the spike protein has been the focus of development for COVID-19 vaccines in response to the COVID-19 pandemic caused by the virus SARS-CoV-2. [11] [12] A subgenus of the betacoronaviruses, known as embecoviruses (not including SARS-like coronaviruses), have an additional shorter surface protein known as hemagglutinin esterase. [13]
Transmission and life-cycle of SARS-CoV-2 causing COVID-19. Coronaviruses vary significantly in risk factor. Some can kill more than 30% of those infected, such as MERS-CoV, and some are relatively harmless, such as the common cold. [49] Coronaviruses can cause colds with major symptoms, such as fever, and a sore throat from swollen adenoids. [91]
SARS-CoV-2 is the seventh known coronavirus to infect people, after 229E, NL63, OC43, HKU1, MERS-CoV, and the original SARS-CoV. [105] Like the SARS-related coronavirus implicated in the 2003 SARS outbreak, SARS‑CoV‑2 is a member of the subgenus Sarbecovirus (beta-CoV lineage B). [106] [107] Coronaviruses undergo frequent recombination. [108]
For instance, SARS-CoV-2, the causative agent of COVID-19, employs its extensively glycosylated spike (S) protein to bind to the ACE2 receptor, allowing it to enter host cells. [3] The spike protein is a trimeric structure, with each subunit containing 22 N-glycosylation sites, making it an attractive target for vaccine search. [3] [4]
M is a glycoprotein whose glycosylation varies according to coronavirus subgroup; N-linked glycosylation is typically found in the alpha and gamma groups while O-linked glycosylation is typically found in the beta group. [8] [9] There are some exceptions; for example, in SARS-CoV, a betacoronavirus, the M protein has one N-glycosylation site.
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