All known life forms translate L-amino acid oligomers from D-nucleic acid templates. Organisms that employ a “mirror image central dogma”—translation of D-proteins from L-nucleic acids—have not been observed, but the bottom-up syntheses of the biochemical components for such mirror-image translation have been reported. The abundance of “mirror glycans,” does not conform to rigid rules of the central dogma. The prevalence of L and D pairs of glycans is different from the prevalence of enantiomers of amino acids and oligonucleotides (1), as confirmed by analysis of glycans across all kingdoms of life. Three factors determine the natural ratio of L and D pairs of glycans: (i) biochemical pathways for the synthesis of monomers, (ii) ability of glycosyl transferases to use them, and (iii) ability to find and characterize such glycans. Recognition of the L and D pairs of glycans by canonical glycan-binding proteins is currently not well understood. However, topological and symmetry analysis of the glycans hints that enantiomers of one glycan contain recognition elements found in another glycan. As a result, enantiomers of common glycans may bind to glycan-binding proteins: components of the plant immune system and innate immune system in mammals. We employ a combination of Machine Learning, total synthesis, glass-based lectin array, and liquid glycan arrays [2] to perform the first comprehensive evaluation of how enantiomeric building blocks in glycobiology are recognized by the same set of glycan-binding proteins [3]. The results from this investigation shed light on fundamental protein-glycan recognition. It outlines the new challenges for ML-based exploration of molecular recognition. By shedding light on immune receptor recognition of mirror image components of the glycocalyx, these data add important information to the discussion of the concept of "mirror image biology" and mirror biology dialogue (https://www.mbdialogues.org/).