Biological macromolecules are utilized in low‐temperature synthetic methods to exert precise control over nanoparticle nucleation and placement. They enable low‐temperature formation of a variety of functional nanostructured materials with properties often not achieved via conventional synthetic techniques. Here we report on the in situ visualization of a novel acidic bacterial recombinant protein, MamC, commonly present in the magnetosome membrane of several magnetotactic bacteria, including Magnetococcus marinus, strain MC‐1. Our findings provide an insight into the self‐assembly of MamC and point to formation of the extended protein surface, which is assumed to play an important role in the formation of biotemplated inorganic nanoparticles. The self‐organization of MamC is compared to the behavior of another acidic recombinant iron‐binding protein, Mms6.

During pregnancy, the maternal body adapts in several ways to create an optimal environment for embryonic growth. These changes include endocrine and metabolic shifts that can lead to insulin resistance and gestational diabetes mellitus (GDM), impacting both the mother and fetus in the short and long term. Fetal macrosomia, a condition where the fetus is significantly larger than average, is a primary concern associated with GDM. Although the underlying mechanism remains unclear, a pregnancy-induced proinflammatory state, combined with altered glucose homeostasis, plays a critical role. Several cytokines and hormones, such as interleukin 6 (IL-6), insulin growth factor 1 (IGF-1), prolactin (PRL), or progesterone, are essential for fetal growth, the control of the inflammatory response, and the regulation of lipid and carbohydrate metabolism to meet energy demands during pregnancy. However, although the role of these cytokines in metabolism and body growth during adulthood has been extensively studied, their implication in the pathophysiology of GDM and macrosomia is not well understood. Here, we review this pathophysiology and pose the hypothesis that an aberrant response to cytokine receptor activation, particularly involving the suppressor of cytokine signaling 2 (SOCS2), contributes to GDM and fetal macrosomia. This novel perspective suggests an unexplored mechanism by which SOCS2 dysregulation could impact pregnancy outcomes.

Magnetotactic bacteria (MTB) biomineralize intracellular magnetite (Fe₃O₄) crystals surrounded by a magnetosome membrane (MM). The MM contains membrane-specific proteins that control Fe₃O₄ mineralization in MTB. Previous studies have demonstrated that Mms13 is a critical protein within the MM. Mms13 can be isolated from the MM fraction of Magnetospirillum magneticum AMB-1 and a Mms13 homolog, MamC, has been shown to control the size and shape of magnetite nanocrystals synthesized in-vitro. The objective of this study was to use several independent methods to definitively determine the localization of native Mms13 in M. magneticum AMB-1. Using Mms13-immunogold labeling and transmission electron microscopy (TEM), we found that Mms13 is localized to the magnetosome chain of M. magneticum AMB-1 cells. Mms13 was detected in direct contact with magnetite crystals or within the MM. Immunofluorescence detection of Mms13 in M. magneticum AMB-1 cells by confocal laser scanning microscopy (CLSM) showed Mms13 localization along the length of the magnetosome chain. Proteins contained within the MM were resolved by SDS-PAGE for Western blot analysis and LC-MS/MS (liquid chromatography with tandem mass spectrometry) protein sequencing. Using Anti-Mms13 antibody, a protein band with a molecular mass of ~14 kDa was detected in the MM fraction only. This polypeptide was digested with trypsin, sequenced by LC-MS/MS and identified as magnetosome protein Mms13. Peptides corresponding to the protein’s putative MM domain and catalytic domain were both identified by LC-MS/MS. Our results (Immunogold TEM, Immunofluorescence CLSM, Western blot, LC-MS/MS), combined with results from previous studies, demonstrate that Mms13 and homolog proteins MamC and Mam12, are localized to the magnetosome chain in MTB belonging to the class Alphaproteobacteria. Because of their shared localization in the MM and highly conserved amino acid sequences, it is likely that MamC, Mam12, and Mms13 share similar roles in the biomineralization of Fe₃O₄ nanocrystals.

Diabetes in pregnancy increases the risk of adverse perinatal outcomes for mother and child, with severity influenced by the type of diabetes and degree of hyperglycemia. This study aimed to identify circulating microRNAs (miRNAs) associated with different types of diabetes in pregnancy. Serum miRNAs were profiled in pregnant South African women with type 1 diabetes (T1DM), type 2 diabetes (T2DM), gestational diabetes (GDM), and normoglycemia using PCR arrays (n = 15). Differentially expressed miRNAs were validated in pregnant South African women (n = 167), and a separate cohort of Spanish pregnant women with T1DM and T2DM (n = 48). PCR arrays showed significant differential expression for miR-19b-3p (↓ 9.8-fold; p = 0.033) in GDM, miR-20a-5p (↓ 4.5-fold; p = 0.047) in T1DM, and miR-29a-3p (↑ 1.8-fold; p = 0.002) in T2DM compared to normoglycemia. Screening in the larger cohort showed lower expression of miR-20a-5p (↓ 2-fold; p = 0.013) in GDM and miR-30d-5p (↓ 2.1-fold; p = 0.032) in T1DM compared to normoglycemia. Additionally, miR-20a-5p levels were higher in women with T2DM compared to those with GDM (↑ 2.5-fold; p = 0.019). Our findings show that miRNA profiles are largely consistent across different types of diabetes in pregnancy, suggesting that hyperglycemia plays a key role in shaping miRNA expressions. Moreover, the identification of several shared gene targets suggests common underlying pathophysiological mechanisms.