Hemolytic Uremic Syndrome: An Increasingly Recognized Public Health Problem

A 28-year-old man was referred and admitted to our hospital due to Escherichia coli O157–mediated hemorrhagic colitis with severe thrombocytopenia. A systemic workup concluded that the patient had acute pancreatitis as well as hemolytic uremic syndrome. The patient was ultimately discharged, with his platelet count having recovered. Our case serves an illustrative example of potentially serious complications of an increasingly recognized public health problem. Systemic studies on this topic are insufficient, and we strongly recommend the further accumulation of more experiences like ours. Several diagnostic and management concerns that emerged in this case are also discussed

B38-CAP is a bacteria-derived ACE2-like enzyme that suppresses hypertension and cardiac dysfunction

Angiotensin-converting enzyme 2 (ACE2) is critically involved in cardiovascular physiology and pathology, and is currently clinically evaluated to treat acute lung failure. Here we show that the B38-CAP, a carboxypeptidase derived from Paenibacillus sp. B38, is an ACE2-like enzyme to decrease angiotensin II levels in mice. In protein 3D structure analysis, B38-CAP homolog shares structural similarity to mammalian ACE2 with low sequence identity. In vitro, recombinant B38-CAP protein catalyzed the conversion of angiotensin II to angiotensin 1–7, as well as other known ACE2 target peptides. Treatment with B38-CAP suppressed angiotensin II-induced hypertension, cardiac hypertrophy, and fibrosis in mice. Moreover, B38-CAP inhibited pressure overload-induced pathological hypertrophy, myocardial fibrosis, and cardiac dysfunction in mice. Our data identify the bacterial B38-CAP as an ACE2-like carboxypeptidase, indicating that evolution has shaped a bacterial carboxypeptidase to a human ACE2-like enzyme. Bacterial engineering could be utilized to design improved protein drugs for hypertension and heart failure