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A single nucleotide polymorphism or SNP is a single nucleotide variation at a specific genomic position in a large population. It is the most prevalent type of sequence variation found in the human genome. Point mutations that occur in more than 1% of the population qualify as SNPs. These are present once every 1000 nucleotides on an average in the human genome. Replacement of a purine with another purine (A/G) or a pyrimidine with another pyrimidine (C/T) is known as a transition. In contrast,...
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During most eukaryotic translation processes, the small 40S ribosome subunit scans an mRNA from its 5' end until it encounters the first start AUG codon. The large 60S ribosomal subunit then joins the smaller one to initiate protein synthesis. The location of the translation initiation is largely determined by the nucleotides near the start codon as there may be multiple translation initiation sites present on the mRNA.  Marilyn Kozak discovered that the sequence RCCAUGG (where R...
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Simple proteins and protein complexes contain only amino acids. In contrast, many other proteins, called conjugated proteins, covalently bond with non-protein moieties.
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Altered host protease determinants for SARS-CoV-2 Omicron.

Jasper Fuk-Woo Chan1,2,3,4,5,6, Xiner Huang1, Bingjie Hu1

  • 1State Key Laboratory of Emerging Infectious Diseases, Department of Microbiology and Carol Yu Centre for Infection, School of Clinical Medicine, Li Ka Shing Faculty of Medicine, The University of Hong Kong, Pokfulam, Hong Kong Special Administrative Region, People's Republic of China.

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Membrane-type matrix metalloproteinases (MT-MMPs) facilitate SARS-CoV-2 entry by cleaving the spike protein and ACE2. Inhibiting MT-MMPs reduces viral replication, revealing new therapeutic targets for severe acute respiratory syndrome coronavirus 2.

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Area of Science:

  • Virology
  • Biochemistry
  • Molecular Biology

Background:

  • Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) infection depends on the proteolytic cleavage of its spike protein.
  • The host enzyme transmembrane protease serine 2 is known to facilitate viral entry, but other proteases involved remain under investigation.

Purpose of the Study:

  • To investigate the role of other host proteases, specifically membrane-type matrix metalloproteinases (MT-MMPs) and a disintegrin and metalloproteinase family members, in SARS-CoV-2 entry.
  • To explore the mechanistic details of MT-MMP involvement in viral entry and replication.
  • To compare the protease usage efficiency between Omicron BA.1 and ancestral SARS-CoV-2 variants.

Main Methods:

  • In vitro and in vivo experiments to assess the impact of MT-MMP inhibition on SARS-CoV-2 replication.
  • Biochemical assays to determine the cleavage activity of MT-MMPs on SARS-CoV-2 spike protein and angiotensin-converting enzyme 2 (ACE2).
  • Comparative analysis of viral entry efficiency using different SARS-CoV-2 variants (Omicron BA.1 and ancestral) and protease inhibitors.

Main Results:

  • Multiple MT-MMP family members and a disintegrin and metalloproteinase family members were identified as capable of mediating SARS-CoV-2 entry.
  • Inhibition of MT-MMPs significantly reduced SARS-CoV-2 replication both in vitro and in vivo.
  • MT-MMPs were shown to cleave the SARS-CoV-2 spike protein and ACE2, facilitating viral fusion.
  • Omicron BA.1 demonstrated increased MT-MMP usage and altered transmembrane serine protease usage for entry compared to the ancestral strain.

Conclusions:

  • MT-MMPs represent significant, previously underappreciated host proteases involved in SARS-CoV-2 infection.
  • Targeting MT-MMPs offers a potential therapeutic strategy to combat SARS-CoV-2.
  • Understanding the differential protease usage by viral variants like Omicron BA.1 provides insights into viral evolution and entry mechanisms.