All consecutive patients who were

All consecutive patients who were confirmatively diagnosed with MP-PPE and TPE, respectively, between January 2008 and December 2016 at Kyungpook National University Hospital, a tertiary referral hospital in South Korea, an area with an intermediate prevalence of active tuberculosis, were enrolled. MP-PPE was diagnosed if all the following criteria were met: the presence of fever, cough, and the infiltration with pleural effusion on a chest imaging; either a single positive serum -specific IgM titer or a 4-fold increase in the -specific IgG titer of convalescent serum with or without a positive -PCR test from any respiratory specimen; exclusion of coinfection with (MTB), other bacteria, or viruses. TPE was confirmed as per criteria used in the previous study. A total of 10 patients were diagnosed with MP-PPE and 275 with TPE during the study period. Among MP-PPE patients, 7 showed a 4-fold increase in the IgG titer of convalescent serum. In the remaining 3, each had a single positive serum IgM titer. Eight patients underwent sputum -PCR test, five of whom tested positive. All showed a clinical and radiological response to bms 5 45 and experienced no other conditions for at least 6 months at follow-up. The TPE patients were diagnosed by a positive MTB culture (n = 240) and pleural tissue histology (n = 35). Lymphocytic effusions, defined as effusion with >50% lymphocytes in the differential leukocyte count of PF, were noted in 8 (80%) patients with MP-PPE and 239 (87%) with TPE, respectively (p = 0.628). Finally, only those patients with lymphocytic effusions were further analyzed. The demographic, laboratory, and radiographic data of both groups are presented in . Patients with MP-PPE were younger than those with TPE (p = 0.001). Serum C-reactive protein (S-CRP) and lactate dehydrogenase (S-LDH) levels were significantly higher in the MP-PPE group than in the TPE group (S-CRP, p = 0.004; S-LDH, p < 0.001), while white blood cell counts were not significantly different between the two groups. In the comparison of PF profiles, the proportion of lymphocyte and levels of protein and ADA were significantly higher in the TPE group than in the MP-PPE group (lymphocyte %, p = 0.006; protein, p < 0.001; ADA, p = 0.003). Total cell counts, glucose concentrations, and LDH levels of PF did not statistically differ between the two groups. Chest radiographic findings revealed that moderate to massive effusions were significantly more frequent in TPE group than in the MP-PPE group (p = 0.004).
Introduction RNA structure is often altered after transcription via enzymatic reactions that modify the component nucleosides. Methylation, acetylation, transglycosylation, and deamination are some of the transformations that occur on nascent RNAs [1–4]. Modified nucleosides in RNA have received considerable attention recently because of new discoveries related to their abundance in mRNA [5,6], their mechanism of incorporation and removal [5–7] and biological function [7–9]. Indeed, the term “epitranscriptomics” has been coined to refer to the study of the biochemical features of a transcriptome not genetically encoded in the ribonucleotide sequence [10,11]. A commonly occurring modified nucleoside in human RNA is inosine (I), the deamination product of adenosine (A) (Fig. 1A) [12]. Inosine presents a pattern of hydrogen bonding sites on its Watson–Crick edge similar to that of guanosine (G). This allows I to preferentially base pair with cytidine (C), even though it lacks G's 2-amino group (Fig. 1B). Thus, adenosine deamination changes the base pairing properties at the site of reaction from a nucleoside (A) that pairs selectively with uridine (U) to one that pairs selectively with C. This change can have a profound effect on RNA structure and function. For instance, deamination of adenosine at specific locations in codons (e.g., UAG stop codon) can change codon meaning (e.g., to UGG tryptophan codon). Indeed, since coding properties of the RNA can be altered by this reaction, adenosine deamination is a type of RNA editing [13]. However, adenosine deamination can modulate RNA properties in ways that are not directly related to an RNA's coding potential. For instance, the A-to-I reaction can alter RNA stability by, for instance, converting an A•C mismatch to the more stable IC pair or by converting an A–U pair to the less stable I•U mismatch. Modulation of RNA properties by adenosine deamination is essential in mammals, and dysfunction in the enzymes responsible leads to disease. In this chapter, we discuss where inosine is found in human RNAs and the family of enzymes responsible for most of the inosine present; the Adenosine Deaminases that act on RNA (ADARs).