mutations in the spike protein have increased the binding affinity of XBB.1.5. The spike protein is the perfect shape to slide into ACE2 receptors, which line many of the cells in our body.

1, which is a hybrid of two BA.2 sublineages. But, XBB.1.5 may be better at binding the human receptor ACE2, the gateway to viral entry into human cells. This "could indicate that the advantage of ...

It has a key mutation at site 486, which allows it to bind more tightly to ACE2, the doors the virus uses to enter our cells. “The mutation is clearly letting XBB.1.5 spread better,” Jesse ...

The mechanism behind XBB.1.5’s increased transmissibility isn’t known for sure. But the subvariant’s F486P mutation allows the virus to more effectively latch onto ACE2 receptors in the body ...

1, XBB.1.5 is a combination of two different versions of the BA.2 subvariant of Omicron. Both parents are particularly good at binding to the ACE2 receptor — the part of the cell the virus ...

The latest subvariant of Omicron sweeping the country, XBB.1.5, is moving fast ... say improves its ability to latch onto the ACE2 receptor; the ACE2 receptor is how the virus gets into our ...

The XBB.1.5 variant features a new mutation at the 486 position of the spike, which is the protein the virus uses to bind to the ACE2 receptor protein on cells in the human respiratory tract.

XBB.1.5 isn’t expected to have more antibody escape than XBB.1 (which already had mutated F486), but it should have greater ACE2 affinity," Bloom recently explained. "So it’s greater ACE2 ...

and strength in binding to ACE2 receptors, where Covid enters cells and infects people. A preprint posted in early January by Chinese researchers focusing on XBB.1.5 argues that it does ...