Several reasons might be considered to explain the higher SNA reactivity of anti-TF Abs in cancer patients: (i) in cancer anti-TF IgM is actually more sialylated due to the altered activity of glycosyltransferases in tumor cells and/or in tumor-bearing host; (ii) the Fab glycans of TF-specific Abs are more accessible to SNA due to IgM conformational modifications after interaction with some ligands, such as MBL or other endogeneous lectins; (iii) the anti-TF IgM sialic acids of controls are masked by some TF-positive ligands that are absent in cancer patients but present in healthy state. Here, TF is linked to neoplasm.