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Enterococcus
Published in Dongyou Liu, Laboratory Models for Foodborne Infections, 2017
While 16S rRNA sequence analysis is valuable for identification of many Enterococcus species (using 97% identity as the threshold), it does not provide adequate resolution between E. casseliflavus and E. gallinarum (which share 99.9% identity). Therefore, other molecular methods are required for routine identification of enterococcal isolates. These include amplification and sequencing of the domain V of the 23S rRNA gene, rRNA or tRNA intergenic spacers, the D-ala:D-ala ligase genes (ddl), the manganese-dependent superoxide dismutase (sodA) genes, the chaperonin 60 (cpn60) gene, the Enterococcus protein A (efaA) gene, genes encoding the RNA polymerase α-subunit (rpoA), the phenylalanyl-tRNA synthase (pheS), and the elongation factor Tu (tufA), in addition to the application of ribotyping, repetitive extragenic palindromic PCR (REP-PCR) or BOX-PCR, pulsed-field gel electrophoresis (PFGE), and multilocus sequence typing (MLST) [3].
Exome sequencing of a Pakistani family with spastic paraplegia identified an 18 bp deletion in the cytochrome B5 domain of FA2H
Published in Neurological Research, 2021
Safdar Abbas, Beatrice Brugger, Muhammad Zubair, Sana Gul, Jasmin Blatterer, Julian Wenninger, Khurram Rehman, Benjamin Tatrai, Muzammil Ahmad Khan, Christian Windpassinger
HSP follows different modes of inheritance such as autosomal dominant, autosomal recessive and X-linked, indicating a detailed phenotypical characterization as a critical step prior to molecular analysis [3, 9]. To date, more than 70 chromosomal loci have been linked to HSP [1, 10–12], in which autosomal dominant HSP accounts for about 38% of cases and autosomal recessive accounts for 53% of cases [13]. Physiologically, the HSP proteins have various functions such as (i) axon transport (e.g., KIF1A and KIF5A), (ii) morphologic role in endoplasmic reticulum (e.g., Atlastin, Spastin and reticulon 2), (iii) physiologic role in mitochondria (e.g., chaperonin 60/heat-shock protein 60, paraplegin and mitochondrial ATP6), (iv) synthesis of myelin (e.g., Proteolipid protein and Connexin 47), (v) protein folding and ER-stress response (e.g., NIPA1, K1AA0196 (Strumpellin), and BSCL2 (Seipin), (vi) corticospinal tract and other neuronal development (e.g., cell adhesion molecule and thyroid transporter MCT8), (vii) fatty acid and phospholipid metabolism (e.g., DDHD1, FA2H, NTE, and CYP2U1); and (viii) endosome membrane trafficking and vesicle formation (e.g., AP4B1, KIAA0415, AP4M1, and AP4E) [see 14,for details]. The clinical heterogeneity of HSP greatly reflects the contribution of diverse cellular pathways in disease pathogenesis [5, 8, 15, 16].