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. 2024 Aug 13:68:e230248.
doi: 10.20945/2359-4292-2023-0248. eCollection 2024.

Decoding the relationship between cow's milk proteins and development of type 1 diabetes mellitus

Luís Jesuino de Oliveira Andrade  1 , Gabriela Correia Matos de Oliveira  2 , Luísa Correia Matos de Oliveira  3 , Alcina Maria Vinhaes Bittencourt  4 , Yvana Baumgarth  1 , Luís Matos de Oliveira  5
Affiliations

Decoding the relationship between cow's milk proteins and development of type 1 diabetes mellitus

Luís Jesuino de Oliveira Andrade et al. Arch Endocrinol Metab. .

Abstract

Objective: To analyze in silico the evidence of molecular mimicry between human beta-cell autoantigens and cow's milk proteins as a potential type 1 diabetes mellitus (T1DM) trigger.

Materials and methods: The in silico analysis was performed using bioinformatics tools to compare the amino acid sequences of cow's milk proteins (bovine serum albumin [BSA] and beta-lactoglobulin [BLG]) and human beta-cell autoantigens (glutamic acid decarboxylase-65 [GAD-65], insulin, and zinc transporter 8 [ZnT8]). The structural and functional characteristics of the proteins were analyzed to identify potential molecular mimicry mechanisms.

Results: The results of the in silico analysis showed significant sequence similarity between BSA/BLG and GAD-65/human insulin/ZnT8, ranging from 19.64% to 27.27%. The cow's milk proteins evaluated shared structural features with the beta-cell antigens selected for comparison, indicating a potential for molecular mimicry between these proteins.

Conclusion: The findings of this study provide further evidence for a potential role of cow's milk proteins in triggering T1DM. The in silico analysis suggests that molecular mimicry mechanisms between cow's milk proteins and human beta-cell antigens may contribute to the autoimmune response leading to T1DM.

Keywords: Type 1 diabetes mellitus; autoantigens; cow’s milk; molecular mimicry.

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Conflict of interest statement

Disclosure: no potential conflict of interest relevant to this article was reported.

Figures

Figure 1
Figure 1. GAD-65 (Q05329 · DCE2_HUMAN) versus BSA (P02769 · ALBU_BOVIN).
Figure 2
Figure 2. GAD-65 (Q05329 · DCE2_HUMAN) versus BLG (P02754 · LACB_BOVIN).
Figure 3
Figure 3. Human insulin (P01308 · INS_HUMAN) versus BLG (P02754 · LACB_BOVIN).
Figure 4
Figure 4. Human insulin (P01308 · INS_HUMAN) versus BSA (P02769 · ALBU_BOVIN).
Figure 5
Figure 5. ZnT8 (Q8IWU4 · ZNT8_HUMAN) versus BLG (P02754 · LACB_BOVIN).
Figure 6
Figure 6. ZnT8 (Q8IWU4 · ZNT8_HUMAN) versus bovine serum albumin (P02769 · ALBU_BOVIN)
Figure 7
Figure 7. Structure alignment analysis between GAD-65 and BSA.
Figure 8
Figure 8. Structure alignment analysis between GAD-65 and BLG.
Figure 9
Figure 9. Structure alignment analysis between human insulin and BLG.
Figure 10
Figure 10. Structure alignment analysis between human insulin and BSA.
Figure 11
Figure 11. Structure alignment analysis between ZnT8 and BLG.
Figure 12
Figure 12. Structure alignment analysis between ZnT8 and BSA.
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