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第七届中国畜牧科技论坛

作者： Chen hongwei Li yinglun Wu junwei Liu juan Huang qingzhou Wei shuyong Zhao guangwei Zhang zhiqiang Hua ling Department of Veterinary Medicine Rongchang CampusSouthwest University College of Veterinary Medicine Sichuan Agricultural University

The aim of this study was to identify theantimicrobial substances in the sacculus rotundus and evaluate their effects on mammalian immune function and molecular *** techniques were used to purify antimicrobial *** with antimicrobial activity were analyzed by NanoLC-ESI-MS/*** mice were given crude protein extract or purified antimicrobial protein by gavage for 4 weeks,and serum cytokine levels were *** lymphocyte proliferation assays were also *** obtained histone cluster 1,H2 bcTike,which had antimicrobial *** termed this protein rabbit sacculus rotundus antimicrobial histone(RSRAH),according to its primary *** analysis and alignment suggested that EKTPVKKKARKSAGAAKRKA was a core segment of the protein mediating its antimicrobial *** with high doses of the crude protein extract for 14,21,and 28 days significantly increased interferon-γ(IFN-γ) levels compared to the ***(IL)-4 levels were also increased significantly on days 7,14,21,and 28 in the experimental ***,treatment with the crude protein extract stimulated a significant increase in lymphocyte proliferation on days 14 and *** of antimicrobial protein isolated from the rabbit sacculus rotundus to immunosuppressed mice increased serum IFN-γ and IL-4 levels and induced lymphocyte proliferation,thereby promoting cellular immune function in immunosuppressed mice.

关键词： sacculus rotundus antimicrobial protein NanoLC-ESI-MS/MS cytokines lymphocyte proliferation

Purification and antifungal activities of an antimicrobial protein LJAMP2 expressed in Pichia pastoris

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Purification and antifungal activities of an antimicrobial p...

重庆市生物化学与分子生物学学术会议

作者： Shaohui Guo,Chengjian Xie,De Wang,Xiaowen Wang,Fei Kou,Xingyong Yang (Key Laboratory of Eco-Environments in Three Gorges Reservoir Region,Ministry of Education, School of Life Science,Southwest University,Chongqing 400716)

LJAMP2,a member of nonspecific lipid transfer protein,isolated from motherwort seeds,displays antimicrobial activity against *** LJAMP2 gene was cloned into the pPIC9K vector and transformed into Pichia pastoris using electrotransformation.A transformant with a high copy number of the gene integrated into the chromosome was obtained by YPD plates which contained 1.75 mg/mL G418.

关键词： motherwort seed antimicrobial protein expression yeast

Isolation and identification of a specific antimicrobial protein from Pseudomonas CMF-2,a bacterium isolated from the jellyfish Cyanea capillata

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Isolation and identification of a specific antimicrobial pro...

全国第九届海洋生物技术与创新药物学术会议

作者： Manman Yin Feng Xu Guoyan Liu Liang Xiao Qianqian Wang Beilei Wang Yinlong Chang Yong Liu Jiemin Zheng Xia Tao Liming Zhang Department of Marine Biotechnology Faculty of Naval MedicineSecond Military Medical University Department of Food Microbiology College of Food Science and EngineeringDalian Ocean University Company Two of the Undergraduate Brigade Second Military Medical University Department ofiPharmacy Changzheng Hospital Second Military Medical University

A bacterium strain,designated as CMF-2,was isolated from the jellyfish Cyanea capillata and its fermentation broth showed a significant antimicrobial *** strain CMF-2was identified as Pseudomonas *** on the morphological,biochemical and physiological characteristics as well as 16S rDNA sequence *** this study,we aimed to isolate the antimicrobial proteins from the culture of CMF-2 through ammonium sulfate precipitation,gel filtration chromatography and anion exchange *** to the result of sodium dodecyl sulfate-polyacrylamide gel electrophoresis(SDS-PAGE)of the purified preparation,a major band suggested that the antimicrobial protein,named as CAP-1,had a molecular mass of about 57 kDa,and it was identified as chaperonin GroEL by MALDI-TOF-MS analysis and Mascot *** protein CAP-1 remained a stable antimicrobial activity in a wide range of temperature(20-100℃)and pH(2-10)*** displayed a broad antimicrobial spectrum against the indicator bacteria and fungus,including Staphylococcus aureus,Escherichia coli,Bacillus subtilis and Candida albicans,especially including some marine-derived microorganisms such as Vibrio vulnificus,Vibrio alginolyticus and Vibrio parahaemolyticus,but showed little impact on tumor cells and human normal skin *** results suggested that CAP-1 might have a specific antimicrobial function not due to cytotoxicity and the Pseudomonas CMF-2 might be a bio-control bacterium of promising research values.

关键词： antimicrobial protein isolation identification antimicrobial activity Cyanea capillata

Purification and antimicrobial Assay of an antimicrobial protein from a Biocontrol Bacterium Strain K2-1 against Aquatic Pathogens

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Purification and Antimicrobial Assay of an Antimicrobial Pro...

福建省海洋学会2014年学术年会暨福建省科协第十四届学术年会

作者： XU Changan TANG Xu LIU Yuansen LIN Ning HUANG Shixin FANG Weidong Third Institute of Oceanography State Oceanic Administration Fishery Department Jimei University Zhangzhou Health Vocational College

In this study,an antimicrobial protein APK2 was purified from a biocontrol bacterium strain *** assay of APK2 in vitro against pathogenic bacterial strains including Vibrio alginolyticus, Aeromonas hydrophila, Aeromonas. Sobria, Pseudomonas fluorescens, Vibrio Parahaemolyticus, Vibrio harveyi and Vibrio anguillarum, was conducted by means of agar diffusion technique. The results show that APK2 had a strong antimicrobial activity against the growth of most those bacteria, suggesting that APK2 could be a potential alternative to replace chemical antimicrobial agent in the control and prevention of aquatic diseases.

关键词： antimicrobial protein purification aquatic pathogen

Purification and antimicrobial Assay of an antimicrobial protein from a Biocontrol Bacterium Strain K2-1 against Aquatic Pathogens

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Agricultural Science & Technology 2015年第8期16卷 1582-1583,1675页

作者：唐旭刘源森林凌黄仕新方卫东徐长安国家海洋局第三海洋研究所福建厦门361005 集美大学水产学院福建厦门361005

[Objective] The aim of this study was to purify an antimicrobial protein from a biocontrol bacterium strain K2-1 and analyze its antimicrobial activity in vitro against some typical aquatic pathogens. [Method] The antimicrobial protein was ob- tained by using ammonium sulfate precipitation and Sephadex chromatography combined with hot water bath. The antimicrobial assay was conducted by means of agar diffusion technique, using Vibrio alginolyticus, Aeromonas hydrophila, Aeromonas. Sobria, Pseudomonas fluorescens, Vibrio Parahaemolyticus, Vibrio har- veyi and Vibrio anguillarum as test bacteria. [Result] antimicrobial protein APK2 can be derived from fermentation broth of strain K2-1 and purified to the chromatogra- phy pure level by the methods provided, the final yield of the antimicrobial compo- nent is approximately 0.08%. This antimicrobial protein had a strong antimicrobial activity against the growth of most those bacteria. [Conclusion] The results show that APK2 could be a potential alternative to replace chemical antimicrobial agent in the control and prevention of aquatic diseases.

关键词： antimicrobial protein Purification Aquatic Pathogen

Bactericidal ability of target acidic phospholipids and phagocytosis of CDC42 GTPase-mediated cytoskeletal rearrangement underlie functional conservation of CXCL12 in vertebrates

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Science China Life Sciences 2024年第12期67卷 2713-2729页

作者： Yanqi Zhang Ning Xia Yazhen Hu Wentao Zhu Chunrong Yang Jianguo Su Hubei Hongshan Laboratory College of Fisheries Huazhong Agricultural University Laboratory for Marine Biology and Biotechnology Qingdao Marine Science and Technology Center School of Marine Sciences Ningbo University College of Veterinary Medicine Huazhong Agricultural University

Chemokine CXCL12 plays a crucial role in both direct bactericidal activity and phagocytosis in humans. However, the mechanisms and evolutionary functions of these processes in vertebrates remain largely unknown. In this study, we found that the direct bactericidal activity of CXCL12 is highly conserved across various vertebrate lineages, including Arctic lamprey(Lampetra japonica), Basking shark(Cetorhinus maximus), grass carp(Ctenopharyngodon idella), Western clawed frog(Xenopus tropicalis), Green anole(Anolis carolinensis), chicken(Gallus gallus), and human(Homo sapiens). CXCL12 also has been shown to promote phagocytosis in lower and higher vertebrates. We then employed C. idella CXCL12a(CiCXCL12a) as a model to further investigate its immune functions and underlying mechanisms. CiCXCL12a exerts direct broad-spectrum antibacterial activity by targeting bacterial acidic phospholipids, resulting in bacterial cell membrane perforation, and eventual lysis. Monocytes/macrophages are attracted to the infection sites for phagocytosis through the rapid production of CiCXCL12a during bacterial infection. CiCXCL12a induces CDC42 and CDC42 GTPase activation, which in turn mediates F-actin polymerization and cytoskeletal rearrangement. The interaction between F-actin and Aeromonas hydrophila facilitates bacterial internalization into monocytes/macrophages. Additionally, A. hydrophila is colocalized within early endosomes, late endosomes and lysosomes, ultimately degrading within phagolysosomes. CiCXCL12a also activates PI3K-AKT, JAK-STAT5 and MAPK-ERK signaling pathways. Notably, only the PI3K-AKT signaling pathway inhibits LPS-induced monocyte/macrophage apoptosis. Thus, CiCXCL12a plays key roles in reducing tissue bacterial loads, attenuating organ injury, and decreasing mortality rates. Altogether, our findings elucidate the conserved mechanisms underlying CXCL12-mediated bactericidal activity and phagocytosis, providing novel perspectives into the immune functions of CXC

关键词： CXCL12 antimicrobial protein actin polymerization apoptosis phagocytosis

Bactericidal/permeability-increasing protein originates in both the testis and the epididymis and localizes in mouse spermatozoa

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Asian Journal of Andrology 2014年第2期16卷 309-313,I0012页

作者： Zhong-Ping Zhou Department of Histology and Embryology Shanghai Jiao Tong University School of Medicine Shanghai Shanghai Key Laboratory of Reproductive Medicine Shanghai China

Bactericidal/permeability-increasing protein （BPI） is an endogenous antibiotic protein with activity against gram-negative bacteria. In the present study, we examined the expression of BPI in postnatal mouse testes and epididymides as well as the subcellular localization within epididymal spermatozoa. Our results showed that, BPI mRNA was expressed in testis and epididymis independently. Throughout the epididymis, the BPI protein level gradually decreased in the epididymal epithelium in a spatial manner, specialized within the cytoplasm of clear cells in the cauda part. We detected BPI proteins in intact acrosome, implying its testicular origin; on the other hand, after the acrosome reaction, BPI proteins were observed dispersed across the entire sperm head, especially enriched at the equatorial segment. Our findings suggested a dual origin of the BPI that generated both in the testis and epididymis, and associated with mouse spermatozoa. BPI protein might be involved in the dynamics modification of the sperm plasma membrane and also the fertilization process.

关键词： acrosome antimicrobial protein bactericidal/permeability-increasing protein epididymis testis

Purification and Characterization of an Antibacterial protein from the Cultured Mycelia of Cordyceps sinensis

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Wuhan University Journal of Natural Sciences 2006年第3期11卷 709-714页

作者： HU Zheng YE Maoqing XIA Liqiu TU Wenjuan LI Liang ZOU Guolin College of Life Sciences Wuhan University Wuhan 430072Hubei China Key Laboratory of Industrial Microbiology of Hubei Province Hubei University of Technology Wuhan 430068 Hubei China College of Life Sciences Hunan Normal University Changsha 410081 Hunan China

An antibacterial protein was isolated from the cultured mycelia of Cordyceps sinensis, and was designated as Cordyceps sinensis Antibacterial protein （CSAP）. CSAP was single-chained, with an apparent molecular mass of 35 × 10^3 revealed by SDS-PAGE and a novel hydrophobic N-terminal sequence N-ALATQHGAP. The antimicrobial assays showed CSAP could inbibit the growth of Gram-positive and Gram-negative bacteria but no significant inhibition against fungi or yeasts. Further more, the antibacterial activity of CSAP was not bactericidal but bacteriostatic. It was the first time that an antibacterial protein was described in the Cordyceps species, which might involve in the chemical defense mechanism of the hosts.

关键词： Cordyceps species antimicrobial protein isolation identification membrane-activity proteins

Enhancing resistance to verticillium wilt by combining expression of antimicrobial proteins(LjAMP1) and chitinase(Bbchit1) in transgenic cotton

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Enhancing resistance to verticillium wilt by combining expre...

第十四届全国植物基因组学大会

作者： Xianbi Li Yanhua Fan Demou Li Yuehua Xiao Ming Luo Lei Hou Shaohui Guo Shuiqing Song Xiaoying Luo Chen Yu Ji Pu Dong Zuo Qian Wu Yan Pei Key Laboratory of Biotechnology and Crop Quality Improvement of Ministry of Agriculture of China Biotechnology Research CenterSouthwest University

Verticillium wilt of cotton is a major factor limiting cotton yield in many cotton-growing areas,and there are no effective chemical controls for the disease. Moreover,in upland cotton(G hirsutum),there is lack of var... 详细信息

关键词： Verticillium wilt antimicrobial protein chitinase transgenic cotton

Cloning and Analysis of TasA Gene in Bacillus subtilis HAS

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Agricultural Biotechnology 2017年第2期6卷 48-50,54页

作者： Guoruo XIONG Gengfeng ZHAO Wenwei CAI Suran WU Benpeng YANG Shuzhen ZHANG Institute of Tropical Biotechnology/Sugarcane Research Center Chinese Academy of Tropical Agricultural Sciences Department of Biochemistry Hainan Medical College

In order to clarify the mechanism for the inhibitory action of the Bacillus subtilis strain HAS on Sporisorium scitamineum （ Syd. ）, which can cause sugarcane smut, the full-length TasA gene which encodes a protein with broad-spectrum antimicrobial activity, was PCR-amplified from HAS, and cloned into pMD18-T vector. Sequence analysis indicated that the full-length TasA cloned from HAS consisted of 786 nucleotides, and shared 99% homology in nucleotide sequence with the TasA gene sequence published in Genbank （AJ871386.1）. It was predicted that the molecular weight of TasA protein was about 28 kD. Base transitions or transversions ~curred at positions 104, 164, 169,250, 399,623 and 627, at the 2nd, 2nd, 3rd , 1st , 3rd, 2nd and 3rd bases of TasA codons. The mutations in the seven bases may cause the missense mutations of the polypeptide chain. Compared with the amino acid sequences of the TasA protein encoded by Bacillus aubtilis subsp, subtilis str. 168, mutations in two amino acids at positions 150 and 209 of the protein encoded by the cloned TasA gene were found, and as a result, an ala- nine was replaced with a threonine.

关键词： Bacillus subtilis HAS mad a glutamic acid was replaced with an asparagine. Sporisorium scitamineum ( Syd. ) antimicrobial protein TasA