Abstract
BackgroundMyelin basic protein (MBP) is one of the most important structural components of the myelin sheaths in both central and peripheral nervous systems. MBP has several functions including organization of the myelin membranes, reorganization of the cytoskeleton during the myelination process, and interaction with the SH3 domain in signaling pathways. Likewise, MBP has been proposed as a marker of demyelination in traumatic brain injury and chemical exposure. MethodsThe aim of this study was to molecularly characterize the myelin basic protein a (mbpa) gene from the Colombian native fish, red-bellied pacu, Piaractus brachypomus. Bioinformatic tools were used to identify the phylogenetic relationships, physicochemical characteristics, exons, intrinsically disordered regions, and conserved domains of the protein. Gene expression was assessed by qPCR in three models corresponding to sublethal chlorpyrifos exposure, acute brain injury, and anesthesia experiments. Resultsmbpa complete open reading frame was identified with 414 nucleotides distributed in 7 exons that encode 137 amino acids. MBPa was recognized as belonging to the myelin basic protein family, closely related with orthologous proteins, and two intrinsically disordered regions were established within the sequence. Gene expression of mbpa was upregulated in the optic chiasm of the chlorpyrifos exposed fish in contrast to the control group. ConclusionsThe physicochemical computed features agree with the biological functions of MBP, and basal gene expression was according to the anatomical distribution in the tissues analyzed. This study is the first molecular characterization of mbpa from the native species Piaractus brachypomus.
Highlights
Myelin basic protein (MBP) is one of the most important structural components of the myelin sheaths in both central and peripheral nervous systems
Myelin basic protein a (MBPa) protein analysis and multiple sequence alignment (MSA) The complete open reading frame (ORF) of mbpa gene from P. brachypomus was detected by Sanger sequencing, with a total length of 414 bp that encodes a protein of 137 amino acids
Seven exons were identified for the teleost MBPa protein, and InterproScan search detected a large region from the residues 1 to 132, corresponding to the Myelin basic protein family (PF01669) (Fig. 1)
Summary
Myelin basic protein (MBP) is one of the most important structural components of the myelin sheaths in both central and peripheral nervous systems. MBP has several functions including organization of the myelin membranes, reorganization of the cytoskeleton during the myelination process, and interaction with the SH3 domain in signaling pathways. Isoforms of classic MPB differ in size and are formed due to alternative splicing of a single mRNA transcript, presenting several different functions among them [7]. In this way, in fish, several MBP cDNAs have been reported [8, 9]. MBPs are necessary for the organization of the myelin membrane, reorganization of the cytoskeleton during the myelination process, and interaction with the SH3 domain in signaling pathways [10,11,12]. MBP has been proposed as a marker of active demyelination in traumatic brain injury (TBI), due to its response to structural damage, and the levels of its gene transcripts change after chlorpyrifos (CPF) exposure and anesthesia [13,14,15]
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