The SP1-77 antibody binds the spike protein at a site that so far has not been mutated in any SARS-CoV-2 variant, broadly neutralizing current variants by a novel mechanism and providing valuable insights for the development of vaccines, according to researchers.

Writing in an August 11 article in Science Immunology, the researchers discuss the broadly neutralizing SP1-77 antibody and their humanized mouse model, which may contribute to identifying therapeutic antibodies against future SARS-CoV-2 variants and other pathogens.

"We hope that this humanized antibody will prove to be as effective at neutralizing SARS-CoV-2 in patients as it has proven to be thus far in preclinical evaluations," Frederick Alt, PhD, from the Program in Cellular and Molecular Medicine at Boston Children's Hospital, who co-led the study, said in a statement.

In related news this week, scientists from Scripps Research reported on August 10 in Science Translational Medicine that they discovered certain antibodies capable of immunity against many different SARS-CoV-2 variants, as well as other SARS viruses like SARS-CoV-1.

Certain animals are more capable of producing these broad antibodies and during their investigation, the study team identified the antibody structures that provide this more comprehensive immune response, which has implications for vaccine production.

In the study, rhesus macaque monkeys were immunized with the SARS-CoV-2 spike protein and two vaccine shots were administered that resemble the current mRNA vaccines available for humans. However, unlike humans, the monkeys had a broad neutralizing antibody response against the virus due to their antibodies recognizing the conserved region, in this case the angiotensin converting enzyme 2 receptor binding site.