Pathology and physiology of Haliotis diversicolor with withering syndrome

Abstract Abalone withering syndrome is a serious chronic disease. Ultrastructure and pathological changes were studied using transmission electron microscopy. Myofibers appeared hollow, and the number of inner intact myofibrils was reduced greatly. The morphology of mitochondria in cells appeared abnormal. Crystal lattice-like inclusions in pathological muscle cells were observed. The hepatopancreas was damaged severely; it was full of empty vesicles and devoid of any recognizable cellular structures. The activities of 3 enzymes, acid phosphatase (ACP), alkaline phosphatase (AKP), and total superoxide dismutase (T-SOD), in hemolymph of healthy and diseased abalone showed little differences. ACP activity in the pedal mucus of healthy and diseased abalone was not significantly different. However, in diseased abalone pedal mucus, activities of AKP and T-SOD were significantly lower than in the control group. In pedal mucus of healthy and diseased abalone, the differential (SDS-PAGE) bands were identified as actin and hemocyanin. Protein identification was accomplished with mass spectrometry. A total of 16 2-DE gel spots were identified; 5 gel spots showed upregulation and 11 gel spots showed downregulation in diseased abalone. Proteins involved in energy production and storage, including fructose-1, 6-bisphosphate aldolase, arginine kinase, and triosephosphate isomerase, showed diverse expression patterns in diseased abalone. For stress-responsive proteins, expression of Cu/Zn-superoxide dismutase showed downregulation. For contraction and regulation proteins of muscle, actin showed significant downregulation. Statement of relevance Abalone withering syndrome (WS) is a serious chronic disease. However, there is limited information on the physiological performance of infected abalones. The present study was to assess the alterations of Haliotis diversicolor caused by WS using transmission electron microscopy as well as assess the immune enzyme activity of hemolymph and mucus, and muscle, mucus proteins changes by 2-DE and SDS-PAGE.