Monoclonal antibody-mediated neutralization of SARS-CoV-2:
The left panel illustrates the morphology of the SARS-CoV-2 virus and displaying the trimeric spike protein on its surface bound with antibodies. The right panel depicts the zoomed view of the trimeric spike protein (top view) in prefusion state bound with monoclonal antibodies. Each monomer of the spike protein shows the receptor binding domain (RBD) in green, orange and magenta, which contains a receptor binding motif in cyan on the top. Mutations emerged in the SARS-CoV-2 Omicron variants are shown in red. Here, the C309 (a parent of VIR-7831 or Sotrovimab) antibody is shown in blue, which is one of the antibodies in clinical use that is minimally impacted by the Omicron variant mutations.
Image Credit: Piyush Prakash, Anshumali Mittal, Vikash Verma, Arun Khatri (CC BY 4.0)
Creationist mode: 
In what may well prove to be a fruitless effort, Anshumali Mittal at the University of Pittsburgh, USA and colleagues have been trying to anticipate how Creationism's beloved pestilential mendacity is likely to modify its SARS-CoV-2 design to make it better at killing people and making others sick, despite the fact that many of them will now have a good degree of immunity, having either been vaccinated against it or acquired it naturally by surviving an earlier attack.
They have been doing so by working out what changes to the spike protein are most likely to enable the virus to evade the antibodies that our immune systems might throw at it in the future
Of course, as any worshiper of the evil genius behind the virus will tell you, it will never give up trying and will always manage to outwit medical science. It's almost exactly like it uses a random process that throws up an almost infinite range of mutations and combinations of mutations, and then something in the environment favours the ones which give most descendants, so even if they are the billion to one chance, the probability that they will arise and become predominant is virtually certain. Rather like repeatedly shuffling the pack and dealing four cards, then repeating until you get four of a kind. It might take days, but if you deal often enough, eventually you will get four of a kind.
Information released ahead of publication in PLOS Pathogens, the PLOS news release explains:
Anshumali Mittal and colleagues describes the structural and functional landscape of neutralizing antibodies against SARS-CoV-2 spike protein and discuss the effects of mutations on the virus spike protein that may allow it to evade antibody responses.
The potency of therapeutic antibodies and vaccines partly depends on how readily the virus can escape neutralization. The SARS-CoV-2 virus will continue to evolve resulting in the emergence of escape variants; therefore, worldwide genomic surveillance, better vaccination drive, development of broadly neutralizing antibodies, and new drugs are vital to combat COVID-19.All viruses mutate as they evolve, and most mutations have either negative or neutral effects on viral fitness. However, some mutations give viruses a selective advantage, making them more infectious, transmittable, and resistant to antibody responses and therapeutics. To better understand the relationship between immune responses to SARS-CoV-2 virus and how mutations may allow the virus to escape neutralization, researchers conducted a review of the literature, comprising approximately 139 studies. They synthesized research on emerging SARS-CoV-2 variants, described the structural basis of how antibodies may neutralize SARS-CoV-2, and mapped out the spike protein mutations or “escape variants” that resist antibody binding and neutralization.
Structure-based escape maps combined with computational modelling are valuable tools to understand how mutations at each residue affect the binding of an antibody, and can be utilized to facilitate the rational design of escape-resistant antibody therapeutics, vaccines and other countermeasures.
The authors
The researchers summarized the structure-based classification of the spike protein receptor-binding domains (RBD) that target antibodies to better understand the molecular mechanisms of neutralization. They also further described the RBD escape mutations for several antibodies that resist vaccine-elicited and therapeutically relevant antibodies binding. Future studies are needed, however, to better understand how these mutations may affect illness severity and mortality.
Creationist mode: 
In the abstract to their paper published open access today in PLOS Pathogens, the authors say:
AbstractNo doubt, Creationist admirers of the sadistic monster which they believe designed the virus and is responsible for modifying it to get around the increasing level of immunity in its target victims, will proudly boast, it will find a way to get round that immunity. Meanwhile, normal people who understand how a natural evolutionary process is responsible for these frequent variants will be hoping that the method the scientists have developed here will give us the ability to be one step ahead of the inevitable evolutionary arms race that such a process inevitably produces, so we can be ready with the next generation of vaccines against the next generation of CARS-CoV-2 viruses, in case they are not only more contagious but also more virulent.
The Severe Acute Respiratory Syndrome Coronavirus 2 (SARS-CoV-2) virus is continuously evolving, and this poses a major threat to antibody therapies and currently authorized Coronavirus Disease 2019 (COVID-19) vaccines. It is therefore of utmost importance to investigate and predict the putative mutations on the spike protein that confer immune evasion. Antibodies are key components of the human immune system's response to SARS-COV-2, and the spike protein is a prime target of neutralizing antibodies (nAbs) as it plays critical roles in host cell recognition, fusion, and virus entry. The potency of therapeutic antibodies and vaccine partly depends on how readily the virus can escape neutralization. Recent structural and functional studies have mapped the epitope landscape of nAbs on the spike protein, which illustrates the footprints of several nAbs and the site of escape mutations. In this review, we discuss (1) the emerging SARS-CoV-2 variants; (2) the structural basis for antibody-mediated neutralization of SARS-CoV-2 and nAb classification; and (3) identification of the RBD escape mutations for several antibodies that resist antibody binding and neutralization. These escape maps are a valuable tool to predict SARS-CoV-2 fitness, and in conjunction with the structures of the spike-nAb complex, they can be utilized to facilitate the rational design of escape-resistant antibody therapeutics and vaccines.
Mittal A, Khattri A, Verma V (2022)
Structural and antigenic variations in the spike protein of emerging SARS-CoV-2 variants.
PLoS Pathog 18(2): e1010260. DOI: 10.1371/journal.ppat.1010260
Copyright: © 2022The authors. Published by PLOS
Open access
Reprinted under a Creative Commons Attribution 4.0 International license (CC BY 4.0)
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