Two "science" revealed: the new coronavirus infection is strong originally there are other key factors.

On October 21st Science, a leading academic journal, published two research papers at the same time, and two teams of scientists from multiple countries found back-to-back that a key, previously unknown factor enhanced the ability of the new coronavirus (SARS-CoV-2) to infect host cells: In addition to the well-known ACE2 complex, another subject on the host cell, called neuropilin-1 (NRP1), also combines with the S protein of the new coronavirus to "pull" the virus into the cell.
this groundbreaking discovery not only helps to understand why the new coronavirus is more infectious and causes more complex symptoms than the SARS virus, but also points to new potential targets and is important for the development of drugs against the new coronavirus.
the new coronavirus is more complex and more propagative than SARS, the researchers note in their paper.
unlike SARS, which is limited to infections in the lower respiratory system, the new coronavirus infects the upper respiratory tract system, including the nasal mucosa, so sneezing can cause the virus to fall off voluntarily and spread rapidly.
, the new crown infection affects a variety of organs, such as the lungs and kidneys, and can cause neurological symptoms, including temporary loss of sense of smell and taste.
this difference has attracted the attention of scientists.
, however, from the process of infecting human cells, both coronavirus recognize and bind the ACE2 binds to human cells, thus opening the door to cells.
s starting point is, why do they cause different diseases when they are also combined with ACE2 subjects?" he said. Professor Mikael Simons of the Technical University of Munich, who heads one of the research teams, said: "It's very important that we have a good time with the
both teams have their sights set on the S protein.
S protein is the "siege hammer" used by the new coronavirus to identify cells, and is the key to the current development of antiviral therapies and vaccines.
S protein with the new coronavirus has a distinct feature different from the SARS virus: it has a Flynn protease cutting bit.
in the human body can therefore cut the new coronavirus S protein into S1 and S2 sub-units.
looking closely at the end sequence after being cut by Flynnase, a small segment of amino acids on the S1 sub-unit caught their attention: from the sequence, this amino acid and the sequence of human proteins combined with NRP-1 were consistent.
, Professor Simons's team used in-body cultured cells to prove that NRP-1 can promote viral infection in the presence of ACE2.
this sequence mutates, NRP1 does not enhance viral infection. The green color in the
image is the human cell infected with the new coronavirus, and without the help of the host factor NPR1, the infection of the virus is greatly reduced (Photo source: Reference 1) "If ACE2 is seen as the door to the cell, then NRP1 may be the factor that brings the virus to the door."
"Professor Simons explains, "In most cells, ACE2 levels of expression are very low, so it is not easy for a virus to find a gate into the cell, and cofactors like NRP-1 may be necessary for the virus."
team also performed autopsies on some of the new crown deaths.
Common olfactory disorders in patients with new crowns, and analysis of samples of nasal tissue in infected people found that highly expressed NRP1 olfactory endocells and olfactory nerve cells were infected with the new coronavirus, further confirming the role of NRP1 in viral infections. Nasal sample tissue in patients with
years of infection with NRP1-positive olfactory endotrine cells (Photo Source: References) Another team led by the University of Bristol in the United Kingdom used a series of structural and bio-chemical methods, which also confirmed the direct interaction between the new coronavirus S protein and NRP1.
More importantly, in in-body cultured human cell lineages, two research teams used single-resistance or selective NRP1 inhibitors for NRP1 to block the interaction between S proteins and NPR1, and the results showed a significant decrease in the infection of the new coronavirus.
the results suggest that "the interaction of the new coronavirus S protein with NRP1 could provide a previously unknown way to contain the COVID-19 pandemic," the researchers concluded in their paper.
" References, James Daly et al., (2020) Neuropilin-1 is a host factor for SARS-CoV-2 infect. Science. DOI: 10.1126/science.abd3072 Science DOI: 10.1126/science.abd2985 . . . Coronavirus: Study finds further door opener into the cell. Retrieved Oct. 21, 2020, from Neuropilin-1 drives SARS-CoV-2 infectivity, findsbly study. Retrieved Oct. 21, 2020, from.