Several seismic reflection surveys were conducted to investigate the seismogenic structure of the 1999 Chi-Chi earthquake (Mw=7.6) in central Taiwan. Two 40 km-long seismic profiles that crossed the area near the epicenter were acquired using the deep reflection method with a targeting depth of 10 km, to search for the decollement boundary. One of the ob tained sections shows a clear reflecdon event that dips to the east by 40° until reaching a depth of 8 km where the earthquake's source was located. This slant event is unambiguously related to the thrusting Chelungpu fault surface. The abundant eastward dipping reflectors on the deep reflection sections faithfully describe thrusting features predicted by the earthquake faulting model. Besides these deep reflections, we also used many shallow seismic reflection lines to delineate the structures in the northern portion of the fault zone, where large ruptures (about 10 m) occurred both on the surface and underground. The 3D structure of the fault surface can be de duced using this cost-effective approach. Although the depth imaged may be limited (e.g., 3 km), shallow seismic data still provides reliable informa tion for the study of large ruptures, and to make better plans for deep wells that might be dr�lled in this area in the future.
Betanodavirus is a causative agent of viral nervous necrosis syndrome in many important aquaculture marine fish larvae, resulting in high global mortality. The coat protein of Betanodavirus is the sole structural protein, and it can assemble the virion particle by itself. In this study, we used a high-titer neutralizing mAB, RG-M18, to identify the linear B-cell epitope on the viral coat protein. By mapping a series of recombinant proteins generated using the E. coli PET expression system, we demonstrated that the linear epitope recognized by RG-M18 is located at the C-terminus of the coat protein, between amino acid residues 195 and 338. To define the minimal epitope region, a set of overlapping peptides were synthesized and evaluated for RG-M18 binding. Such analysis identified the 195VNVSVLCR202 motif as the minimal epitope. Comparative analysis of Alanine scanning mutagenesis with dot-blotting and ELISA revealed that Valine197, Valine199, and Cysteine201 are critical for antibody binding. Substitution of Leucine200 in the RGNNV, BFNNV, and TPNNV genotypes with Methionine200 (thereby simulating the SJNNV genotype) did not affect binding affinity, implying that RG-M18 can recognize all genotypes of Betanodaviruses. In competition experiments, synthetic multiple antigen peptides of this epitope dramatically suppressed giant grouper nervous necrosis virus (GGNNV) propagation in grouper brain cells. The data provide new insights into the protective mechanism of this neutralizing mAB, with broader implications for Betanodavirus vaccinology and antiviral peptide drug development.
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