Coronavirus (1407) Science: Structural basis for continued antibody evasion by the SARS-CoV-2 receptor binding domain

5 December, 2021

Dear Colleagues,

I am sharing an important publication on how evasive SARS-CoV2 has been, just published by Science: [*see note below]

Best wishes and keep safe,


HIFA profile: Enku Kebede-Francis (PHD, MS, MEd) is an advisor in global health governance. She has worked for the United Nations (UNESCO, UNDP, UNFPA and UNDPI); was an Assistant Professor at Tufts University Medical School/Department of Public Health; and, a Visiting Scientist at the USDA's Center for Human Nutrition Research Center for Aging and a Visiting Fellow at the Australian National University Medical School. She also designed and implemented preventive health programs promoting women’s health and tobacco cessation programs in Croatia and worked on addiction prevention programs in Florida and Massachusetts, USA. Her professional interests include preventing scurvy and childhood blindness in developing countries using micronutrients. An advocate for primary healthcare for all as a right, she published a textbook in 2010, Global health Disparities: closing the gap through good governance.

[*Note from HIFA moderator (Neil PW): For the benefit of those who may not have immediate web access, here is the abstract: 'Many studies have examined the impact of SARS-CoV-2 variants on neutralizing antibody activity after they have become dominant strains. Here, we evaluate the consequences of further viral evolution. We demonstrate mechanisms through which the SARS-CoV-2 receptor binding domain (RBD) can tolerate large numbers of simultaneous antibody escape mutations and show that pseudotypes containing up to seven mutations, as opposed to the one to three found in previously studied variants of concern, are more resistant to neutralization by therapeutic antibodies and serum from vaccine recipients. We identify an antibody that binds the RBD core to neutralize pseudotypes for all tested variants but show that the RBD can acquire an N-linked glycan to escape neutralization. Our findings portend continued emergence of escape variants as SARS-CoV-2 adapts to humans.']