Women are protected by protein that lets in coronavirus


The human enzyme ACE2, which enables the novel coronavirus to infect the cell, is also key in protecting against cardiovascular, lung and kidney diseases

  • The new research has found; it may be offering protection to women against Covid-19 disease.
  • The research has looked at why female COVID-19 patients face less severe disease complications and a lower risk of dying than male patients, and found that it is hormones and chromosomes that contribute to a stronger immune response.
  • And the highlight of the study is how the sex differences in Covid-19 are linked to ACE2.
  • Because of their chromosomes, women have two copies of the ACE2 gene and men have only one copy. 
  • This does not seem to make women more susceptible to Covid-19 infection, the research found, it rather protects them from the complications associated with the virus.
  • ACE2 is a gene linked to the X chromosome. And women have twice as many active genetic instructions to make ACE2
  • Research is underway to understand how manipulating ACE2 levels might help Covid-19 patients, to prevent infection by blocking the enzyme, or to protect the body by enhancing it.


Enzyme ACE2:

  • Angiotensin-converting enzyme 2 (ACE2) is an enzyme attached to the cell membranes of cells located in the lungs, arteries, heart, kidney, and intestines
  • ACE2 lowers blood pressure by catalyzing the hydrolysis of angiotensin II (a vasoconstrictor peptide) into angiotensin (1–7) (a vasodilator). 
  • ACE2 counters the activity of the related angiotensin-converting enzyme (ACE) by reducing the amount of angiotensin-II and increasing Ang(1-7), making it a promising drug target for treating cardiovascular diseases. 
  • ACE2 also serves as the entry point into cells for some coronaviruses, including HCoV-NL63, SARS-CoV, and SARS-CoV-2.
  • The human version of the enzyme is often referred to as hACE2.



  • Angiotensin-converting enzyme 2 is a zinc-containing metallo enzyme located on the surface of endothelial and other cells
  • ACE2 protein contains an N-terminal peptidase M2 domain and a C-terminal collectrin renal amino acid transporter domain. 
  • ACE2 is a single-pass type I membrane protein, with its enzymatically active domain exposed on the surface of cells in the lungs and other tissues. 
  • The extracellular domain of ACE2 is cleaved from the transmembrane domain by another enzyme known as sheddase, and the resulting soluble protein is released into the bloodstream and ultimately excreted as urine.



  • The primary function of ACE2 is to act as a counterbalance to the Angiotensin-converting enzyme (ACE). 
  • ACE cleaves angiotensin I hormone into the vasoconstricting angiotensin II. 
  • ACE2, in turn, cleaves the carboxyl-terminal amino acid phenylalanine from angiotensin II (Asp-Arg-Val-Tyr-Ile-His-Pro-Phe) and hydrolyses it into the vasodilator angiotensin (1-7), (H-Asp-Arg-Val-Tyr-Ile-His-Pro-OH). 
  • ACE2 can also cleave numerous peptides, including [des-Arg9]- bradykinin, apelin, neurotensin, dynorphin A, and ghrelin. 
  • ACE2 also regulates the membrane trafficking of the neutral amino acid transporter SLC6A19 and has been implicated in Hartnup's disease. 
  • Research in mice has shown that ACE2 is involved in regulation of the blood glucose level but its mechanism is yet to be confirmed.
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