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" ... Antibodies targeting the receptor-binding motif and ACE2 contact epitopes neutralize SARS-CoV-2 effectively but fail to effectively neutralize many of the variants and all of the non-SARS-CoV-2 viruses. There is one exception, S2E12, which both neutralizes a broad range of viruses and which is unaffected by almost all amino acid substitutions in the receptor-binding domain. The S2E12 exception is attributed to the recognition of contacts between the subunits of the trimeric receptor that are constrained to maintain consistent protein interactions even though individual Aino acids at the contact points may vary. ... "
" ... Broadly neutralizing means a given antibody is able to effectively bind and neutralize a broad range of structurally related epitopes (bits of antigens that bind paratopes, specific counterparts of antibodies), typically from related strains and subtypes of a given pathogen such as flu. In the form of a broad adaptive immune response, bnAb has thus come to represent a holy grail of sorts in diseases such as flu, HIV, HCV that currently lack effective, long-lasting vaccines. ... "
" ... The deletions in the N-terminal domain are most likely to delete neutralizing antibody epitopes, while maintaining the function of the entire S1 protein. On the other hand, all the mutations in the receptor binding domain are point mutations, or substitutions, which may affect immunogenicity and affinity but leave existing functions intact. This region seems to be intolerant of deletions. D614G, a mutation that became dominant last spring and forewarned the current explosion in variation, is one example. On the whole, the mutations in the receptor binding domain are more striking, if only because more parallels exist between them and the new variants threatening populations the world over. ... "
" ... To examine naturally occurring antibodies that recognize these epitopes, they identified those linear regions which are recognized by convalescent sera. The figure below shows the regions in which naturally occurring convalescent antibodies bind linear epitopes (Figure 2). It is important to note that these are very different from what is seen when the entire spike protein or receptor-binding domain is used as a target. When the spike protein or receptor-binding domain are targeted, the recognized structures are three-dimensional and yield different binding actions. Whereas in this study, linear epitopes are recognized and the receptor-binding domain is nearly ignored. This is notable as the receptor-binding domain is the principal source for neutralizing monoclonal antibodies in most previous studies. Additionally, antibody responses vary from patient to patient, as no two immune responses are identical. ... "