We investigated the gut microbiota in patients with non-alcoholic fatty liver disease (NAFLD) and its correlation with fibrosis and steatosis stratified by body mass index, as reflected in the controlled attenuation parameter and transient elastography values. A cross-sectional study was performed on 37 patients with NAFLD at Cipto Mangunkusumo National General Hospital from December 2018 to March 2019. The gut microbiota was investigated in fecal samples with 16S RNA sequencing using the MiSeq next-generation sequencing platform (Illumina). NAFLD was more common in patients with metabolic syndrome. Firmicutes, Bacteroidetes, and Proteobacteria were the predominant phyla. Bacteroides was more dominant than Prevotella, contrary to the results of previous studies on healthy populations in Indonesia. Microbiota dysbiosis was observed in most samples. The gastrointestinal microbiota diversity was significantly decreased in patients with NAFLD, high triglyceride levels, and central obesity. The Firmicutes/Bacteroidetes ratio correlated with steatosis and obesity, whereas some of the other species in lower taxonomy levels were mostly associated with steatosis and obesity without fibrosis. Proteobacteria was the only phylum strongly correlated with fibrosis in patients with an average body mass index. The gut microbiota diversity was decreased in patients with NAFLD, high triglyceride levels, and central obesity, and certain gut microbes were correlated with fibrosis and steatosis.
Nonalcoholic fatty liver disease (NAFLD) is a hepatic manifestation of metabolic syndrome. Its prevalence increases with increasing rates of obesity, insulin resistance, and diabetes mellitus. The pathogenesis of NAFLD involves many factors, including the gastrointestinal microbiota. However, there is still debate about the impact of gut dysbiosis in the NAFLD disease progression. Therefore, this paper aims to review the relationship between gut microbiota and other risk factors for NAFLD and how gut dysbiosis plays a role in the pathogenesis of NAFLD. Hopefully, this paper can make an appropriate contribution to the development of NAFLD research in the future.
Based on genetic and antigenic differences and on their cell tropism, human herpes virus-6 (HHV-6) has been classified into two variants, HHV-6A and HHV-6B. Recently, these variants were re-classified as two different species. The HHV-6A glycoprotein complex, gH/gL/gQ1/gQ2 binds to its cellular receptor, CD46; however, the corresponding complex in HHV-6B rarely binds to CD46. To determine which viral molecules in the glycoprotein complex determine HHV-6A-CD46 binding, each molecule of the HHV-6A complex (i.e., gH, gL, gQ1, or gQ2) was replaced with the corresponding HHV-6B molecule, and the ability of the replaced protein to be incorporated into the complex and the ability of the complex to bind CD46 were examined. It was found that when all four glycoproteins were expressed, they were able to form a tetrameric complex. However, a complex formed by HHV-6A gH/gL/ gQ1/gQ2 complexes replaced with HHV-6B gQ1 or gQ2 scarcely bind CD46, whereas HHV-6A complexes in which gH or gL was replaced with the HHV-6B molecules did bind it. These results indicate that HHV-6A gQ1 and gQ2 play an important role in CD46 binding.Key words CD46 antigen, glycoprotein Q1, glycoprotein Q2, human herpesvirus-6A and -6B.Human herpesvirus 6 (HHV-6) belongs to the betaherpesvirus subfamily (1). It was first isolated from peripheral blood lymphocytes of patients with lymphoproliferative disorders (2). Based on their genetic and antigenic differences and their cell tropism, HHV-6 isolates were classified into two variants, HHV-6A and HHV-6B (2-5). Recently, HHV-6A and HHV-6B were re-classified as different species (see the Virus Taxonomy List 2011; reference (6)). Primary infections with HHV-6B cause exanthem subitum (7). The diseases caused by HHV-6A, if any, are unknown. Although the homology between the HHV-6A and -6B is almost 90% over their entire genome, HHV-6A can infect a greater variety of human cells than HHV-6B (8-11). However, which HHV-6 genes are responsible for the differences between HHV-6A and HHV-6B in cell tropism remains unclear.Human CD46 is a cellular receptor of HHV-6 (12) and its viral ligand is a glycoprotein complex made up of viral gH/gL/gQ1/gQ2 (13). Studies using neutralizing antibodies against HHV-6A/B gQ1 have shown that gQ1 plays an important role in viral entry (14,15). In herpesviruses, formation of the gH/gL heterodimer is critical for viral function (16). In HHV-6A, the gH/gL heterodimer requires the additional association of gQ1 and gQ2 (13) for the trafficking and receptor binding of this complex (17). HHV-6B gH/gL also associates with the gQ1/gQ2 complex (14); however, the HHV-6A gH/ gL/gQ1/gQ2 complex binds to its human cellular receptor, CD46, whereas the corresponding complex in some HHV-6B strains seems not to bind it (8, 13). More recently, we found that human CD134 functions as a specific receptor for HHV-6B, but not for HHV-6A, and † Chyntia Jasirwan, Yoshikazu Furusawa and Huamin Tang contributed equally to this study. List of Abbreviations: a.a., amino acid; CBMC, umbilical cord blood mo...
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