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Zhou Z.,Guangdong Ocean University | Zhou Z.,Guangdong Provincial Key Laboratory of Pathogenic Biology | Zhou Z.,Key Laboratory Of Control For Diseases Of Aquatic Economic Animals Of Guangdong Higher Edu Institute | Pang H.,Guangdong Ocean University | And 17 more authors.
Fish and Shellfish Immunology

Type III secretion system (T3SS) in Vibrio alginolyticus is essential for its pathogenesis. VscO's homologous proteins FliJ, InvI and YscO have been suggested to be putative chaperone escorts although its function in V. alginolyticus is unclear. To investigate the physiological role of VscO, a mutant strain of V. alginolyticus with an in-frame deletion of the vscO gene was constructed in the present study. One finding was that the mRNA expression levels of SycD, VopB and VopD proteins decreased in the δ. vscO mutant. In addition, the δ. vscO mutant showed an attenuated swarming ability and a ten-fold decrease in the virulence to fish. However, the δ. vscO mutant showed no difference in the biofilm formation and ECPase activity. Complementation of the mutant strain with the vscO gene could restore the phenotypes of the wild-type strain. Finally, the recombinant VscO protein caused a high antibody titer and an effective protection against lethal challenge with the wild-type strain V. alginolyticus. These results indicated that VscO protein has a specific role in the pathogenesis of V. alginolyticus and it may be a candidate antigen for development of a subunit vaccine against vibriosis. © 2013 Elsevier Ltd. Source

Pang H.-Y.,Guangdong Ocean University | Pang H.-Y.,Guangdong Provincial Key Laboratory of Pathogenic Biology | Pang H.-Y.,Economic Animals of Guangdong Higher Education Institutes | Zhang X.-Z.,Guangdong Ocean University | And 14 more authors.
Aquaculture Research

Vibrio alginolyticus is one of the most serious diseases in cultured marine and freshwater fish and shellfish. The absence of suitable vaccine or virulent marker can be the bottleneck to control V. alginolyticus infection. In this study, immunoproteomic approaches were undertaken to study the immunogenicity of the whole-cell protein of V. alginolyticus HY9901. The whole-cell proteins were analysed by two-dimensional gel electrophoresis and subsequent immunoblotting using the rabbit anti-V. alginolyticus HY9901 serum. A total of 55 immunogenic proteins were identified by immunoproteomic analysis. Of the 55 proteins, 51 are specific immunoreactive proteins and four are nonspecific immunoreactive proteins. Furthermore, outer membrane protein N (spot 2) was used as immunogens to immunize Epinephelus coioides for investigation of protective abilities and activities. The E. coioides immunized with OmpN has abilities to fight against infections caused by V. alginolyticus. The other novel immunogenic proteins may be developed as alternative antigens for further study of V. alginolyticus vaccine and diagnostics. These data show that immunoproteomics methods can be successfully applied in identifying immunogenic proteins of V. alginolyticus, which helps to search for the protective antigens in future. © 2012 Blackwell Publishing Ltd. Source

Yang S.-P.,Guangdong Ocean University | Yang S.-P.,Guangdong Provincial Key Laboratory of Pathogenic Biology | Wu Z.-H.,Guangdong Provincial Key Laboratory of Pathogenic Biology | Wu Z.-H.,Zhongkai University of Agriculture and Engineering | And 2 more authors.
Israeli Journal of Aquaculture - Bamidgeh

The effects of orally-administered dry and live marine red yeast Rhodosporidium paludigenum on antioxidant-related gene expression in the hepatopancreas and hemocytes of Litopenaeus vannamei were investigated by RT-PCR. In the hepatopancreas of L. vannamei fed dry yeast, manganese superoxidate dismutase (SODMn) and catalase (CAT) were enhanced while glutathione peroxidase (GPx) and ferritin remained at the same levels as in the control group. In the hepatopancreas of L. vannamei fed live yeast, SODMn and ferritin were higher than in the control. In hemocytes of L. vannamei fed dry yeast, SODMn was lower, ferritin was similar, and CAT and GPx fluctuated, in comparison to the control. In hemocytes of L. vannamei fed live yeast, SODMn was lower, ferritin was higher, and CAT and GPx tended to be lower than in the control group. Results suggest that consumption of the marine red yeast, R. paludigenum, can stimulate antioxidant gene expression in the hepatopancreas of shrimp. Source

Cai S.H.,Guangdong Ocean University | Cai S.H.,Guangdong Provincial Key Laboratory of Pathogenic Biology | Cai S.H.,Economic Animals of Guangdong Higher Education Institutes | Lu Y.S.,Guangdong Ocean University | And 8 more authors.
Journal of Fish Diseases

The outer membrane proteins of the marine aquatic animal pathogen, Vibrio alginolyticus, play an important role in the virulence of the bacterium and are potential candidates for vaccine development. In this study, the gene encoding an outer membrane protein-OmpU was cloned and expressed in Escherichia coli. Polyclonal antibodies were raised in rabbits against the purified recombinant OmpU, and the reaction of the antibody was confirmed by Western blotting using the isolated OmpU and the recombinant OmpU of V. alginolyticus. To analyze the immunogenicity of the recombinant OmpU, crimson snapper, Lutjanus erythropterus Bloch, were immunized by intraperitoneal injection, and antibody response was assessed by the enzyme-linked immunosorbent assay (ELISA). The results demonstrated that the recombinant OmpU produced an observable antibody response in all sera of the vaccinated fish. The vaccinated fish were challenged by virulent V. alginolyticus and observed to have high resistance to infection. These results indicate that the recombinant OmpU is an effective vaccine candidate against V. alginolyticus in L. erythropterus. © 2013 Blackwell Publishing Ltd. Source

Gan Z.,Guangdong Ocean University | Gan Z.,Guangdong Provincial Key Laboratory of Pathogenic Biology | Gan Z.,Key Laboratory of Control for Disease of Aquatic Animals of Guangdong Higher Education Institutes | Wang B.,Guangdong Ocean University | And 17 more authors.

CD2BP2 (CD2 cytoplasmic tail binding protein 2), one of several proteins interacting with the cytoplasmic tail of CD2, plays a crucial role in CD2-triggered T cell activation and nuclear splicing. The studies on CD2BP2 have tended to be confined to a few mammals, and little information is available to date regarding fish CD2BP2. In this paper, a CD2BP2 gene (On-CD2BP2) was cloned from Nile tilapia, Oreochromis niloticus. Sequence analysis showed that the full length of On-CD2BP2 cDNA was 1429. bp, containing a 5'untranslated region (UTR) of 111. bp, a 3'-UTR of 193. bp and an open reading frame of 1125. bp which is encoding 374 amino acids. Two important structural features, a GYF domain and a consensus motif GPFXXXXMXXWXXXGYF were detected in the deduced amino acid sequence of On-CD2BP2, and the deduced genomic structure of On-CD2BP2 was similar to the known CD2BP2. The mRNA expression of On-CD2BP2 in various tissues of Nile tilapia was analyzed by fluorescent quantitative real-time PCR. In healthy Nile tilapia, the On-CD2BP2 transcripts were mainly detected in the head kidney and spleen. While vaccinated with inactivated Streptococcus agalactiae, the On-CD2BP2 mRNA expression was significantly up-regulated in the head kidney, spleen and brain 48. h post immunization. Moreover, there was a clear time-dependent expression pattern of On-CD2BP2 after immunization and the expression reached the highest level at 24. h in the brain and 48. h in the head kidney and spleen. This is the first report of proving the presence of a CD2BP2 ortholog in fish, and investigating its tissue distribution and expression profile in response to bacterial stimulus. These findings indicated that On-CD2BP2 may play an important role in the immune response to bacteria in Nile tilapia. © 2014 Elsevier B.V. Source

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