-Background -Exposure to viral antigens that share amino acid sequence similar with self-antigens might trigger autoimmune diseases in genetically predisposed individuals, and the molecular mimicry theory suggests that epitope mimicry between the virus and human proteins can activate autoimmune disease. Objective -The purpose of this study is to explore the possible sequence similarity between the amino acid sequences of thyroid self-protein and hepatitis C virus proteins, using databanks of proteins and immunogenic peptides, to explain autoimmune thyroid disease. Methods -Were performed the comparisons between the amino acid sequence of the hepatitis C virus polyprotein and thyroid self-protein human, available in the database of National Center for Biotechnology Information on Basic Local Alignment Search Tool. Results -The sequence similarity was related each hepatitis C virus genotype to each thyroid antigen. The similarities between the thyroid and the viral peptides ranged from 21.0 % (31 identical residues out of 147 amino acid in the sequence) to 71.0% (5 identical residues out of 7 amino acid in the sequence). Conclusion -Bioinformatics data, suggest a possible pathogenic link between hepatitis C virus and autoimmune thyroid disease. Through of molecular mimicry is observed that sequences similarities between viral polyproteins and self-proteins thyroid could be a mechanism of induction of crossover immune response to self-antigens, with a breakdown of self-tolerance, resulting in autoimmune thyroid disease. HEADINGS -Hepacivirus. Thyroiditis. Amino acid sequence homology. Computational biology.
Background: Thyroid-stimulating hormone (TSH) is a member of the vertebrate glycoprotein hormone family [1]. It’s secreted from pituitary cells as heterodimers composed of an alpha and a beta- subunit. The thyrotrophic cells that secrete TSH are preferentially located in the anteromedial and anterolateral portions of the pituitary. Objective: We performed a phylogenetic analysis of the TSH, and phylogram of the maximum likelihood relations between TSH coding sequences of five representative species. Methods: We extracted the available DNA and protein sequences for TSH from the NCBI databank. Searched for regions presenting sequence similarities to the constituent domains of TSH – alpha and beta-subunits - with the Blastall command ftp://ftp.ncbi.nlm.nih.gov/blast/db/ website, pairs of sequences were compared on the basis of their global alignment with the Myers & Millers algorithm manpages.ubuntu. com/manpages/karmic/man1, and the phylogenetic reconstructions were performed online by using a maximum likelihood method with PhyMyL 3.0 software on the website file (http://www.phylogeny.fr/). Results: The comparison of the phylogenetic trees that we obtained compared with those studies previously published revealed similar subclusters with high protein homology. Conclusion: This study demonstrates that human TSH is structurally related to TSH of the species analysed, Bos taurus, Mus musculus, Canis lupus familiaris, and Cyprinus carpio, respectively.
<p><strong>Introduction</strong>: the severe acute respiratory syndrome – coronavirus 2 (SARS Cov-2), leads to a diffuse alveolar deterioration due infection of type II pneumocytes. The type II pneumocytes are involved in synthesis and secretion of pulmonary surfactant in pulmonary alveoli. <strong>Objective</strong>: the purpose of this study is to discuss the indication of surfactant replacement as a potential adjunctive treatment modality for SARS CoV-2, similarly treatment to neonatal respiratory distress syndrome. <strong>Methodology</strong>: we argue that SARS can be triggered by surfactant deficiency secondary to production deficiency determined by type 2 pneumocyte injuries. In this sense, we carried out a bibliographic review. <strong>Conclusion</strong>: thus, the replacement of human surfactant could be a potential treatment modality for SARS CoV-2, in the same way that it is indicated for the treatment of neonatal respiratory distress syndrome</p>
Introduction: Introduction: Type 1 diabetes mellitus (T1DM) is an autoimmune disease that develops due to the destruction of insulin-producing beta-cells in the pancreas by the immune system. Cow milk is one of the dietary factors associated with the development of T1DM, as it contains proteins that may trigger the autoimmune response. Objective: To analyze in silico the evidence of molecular mimicry between Glutamic Acid Decarboxylase-65 (GAD-65)/ Human insulin/Zinc Transporter 8 (ZnT8) and bovine serum albumin (BSA) and beta-lactoglobulin (BLG) as a potential trigger for T1DM. Method: The in silicoanalysis was performed using bioinformatics tools to compare the amino acid sequences of cow milk proteins (BSA and BLG) and human beta-cell autoantigens (GAD-65, Human insulin and 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 and 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 the potential for molecular mimicry between these proteins. Conclusion: The findings of this study provide further evidence for the potential role of cow milk proteins in the triggering of T1DM. The in silico analysis suggests that molecular mimicry mechanisms between cow milk proteins and human beta-cell antigens may contribute to the autoimmune response that leads to T1DM. This study highlights the importance of dietary factors in the development of T1DM and the need for further research to understand the mechanisms involved.
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