The supply of relevant immunological components is stable throughout the colostrum stage. The effects of pasteurization on antibodies depend on isotype, subclass, and specificity. This information is relevant to improving the immunological quality of colostrum, especially for preterm newborns.

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Enamel defects in permanent and deciduous teeth may be oral manifestations of celiac disease. Sometimes they are the only sign that points to this underdiagnosed autoimmune pathology. However, the etiology of these specific enamel defects remains unknown. Based on previously reported cross-reactivity of antibodies to gliadin with the enamel proteins, amelogenin and ameloblastin, we analyzed (using immunohistochemistry) the ability of anti-gliadin IgG, produced during untreated disease, to recognize enamel organ structures. We used swine germ teeth as a tissue model because they are highly homologous to human teeth in terms of proteins and development biology. Strong staining of the enamel matrix and of the layer of ameloblasts was observed with serum samples from women with celiac disease; high IgG reactivity was found against both gliadin peptides and enamel matrix protein extract, but there was no IgG reactivity against tissue antigens. In line with these findings, the gamma globulin fraction from gliadin-immunized BALB/c mice showed a similar staining pattern to that of amelogenin-specific staining. These results strongly suggest a pathological role for antibodies to gliadin in enamel defect dentition for both deciduous and permanent teeth, considering that IgG can be transported through the placenta during fetal tooth development.

Human milk (HM) constitutes the first immunological barrier and the main source of nutrients and bioactive components for newborns. Immune factors comprise up to 10% of the protein content in HM, where antibodies are the major components (mainly IgA, IgG, and IgM). In addition, antibacterial enzymes such as lysozyme and immunoregulatory factors such as soluble cluster of differentiation 14 (sCD14) and transforming growth factor β2 (TGF-β2) are also present and play important roles in the protection of the infant's health. Donor milk processed in HM banks by Holder pasteurization (HoP; 62.5°C, 30 min) is a safe and valuable resource for preterm newborns that are hospitalized, but is reduced in major immunological components due to thermal inactivation. We hypothesized that high hydrostatic pressure (HHP) and high-pressure homogenization (HPH) are 2 processes that can be used on HM to reduce total bacteria counts while retaining immunological components. We studied the effects of HHP (400, 450, and 500 MPa for 5 min applied at 20°C) and HPH (200, 250, and 300 MPa, milk inlet temperature of 20°C) applied to mature HM, on microbiological and immunological markers (IgA, IgG, IgM, sCD14, and TGF-β2), and compared them with those of traditional HoP in HM samples from healthy donors. The HHP processing between 400 and 500 MPa at 20°C reduced counts of coliform and total aerobic bacteria to undetectable levels (<1.0 log cfu/mL) while achieving approximately 100% of immunological component retention. In particular, comparing median percentages of retention of immunological components for 450 MPa versus HoP, we found 101.5 versus 50.5% for IgA, 89.5 versus 26.0% for IgM, 104.5 versus 75.5% for IgG, 125.0 versus 72.5% for lysozyme, 50.6 versus 0.1% for sCD14, and 88.5 versus 61.1% for TGF-β2, respectively. Regarding HPH processing, at a pressure of 250 MPa and inlet temperature of 20°C, the process showed good potential to reduce coliforms to undetectable levels and total aerobic bacteria to levels slightly above those obtained by HoP. The median percentages of retention of immunological markers for HPH versus HoP were 71.5 versus 52.0%, 71.0 versus 27.0%, 104.0 versus 66.5%, and 30.9 versus 0.2%, for IgA, IgM, IgG, and sCD14, respectively; results did not significantly differ for lysozyme and TGF-β2. The HPH at 300 MPa produced higher inactivation of immunological components, similar to values achieved with HoP.

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