Journal of Microbiology

Journal Articles

Physiological roles of catalases Cat1 and Cat2 in Myxococcus xanthus: Kimura Yoshio , Yuri Yoshioka , Kie Toshikuni; J. Microbiol. 2022;60(12):1168-1177. Published online October 24, 2022; DOI: https://doi.org/10.1007/s12275-022-2277-7

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Catalases are key antioxidant enzymes in aerobic organisms. Myxococcus xanthus expresses two monofunctional catalases, small-subunit Cat1 and large-subunit Cat2. The Km of H2O2 for recombinant Cat1 and Cat2 were 14.0 and 9.0 mM, respectively, and the catalytic efficiency of Cat2 (kcat/Km = 500 sec-1 mM-1) was 4-fold higher than that of Cat1. The activity ratio of Cat1 to Cat2 in the exponential growth phase of M. xanthus was 1 to 3–4. A Cat1-deficient strain was constructed, whereas a Cat2-deficient strain could not be produced. In H2O2-supplemented medium, the cat1 mutant exhibited marked growth retardation and a longer generation time than the wild-type (wt) strain. After 2 h of incubation in 0.5 mM H2O2-supplemented medium, the catalase activity of the wt strain significantly increased (by 64-fold), but that of the cat1 mutant strain did not. Under starvation-induced developmental conditions, catalase activity was induced by approximately 200-fold in both wt and cat1 strains, although in the mutant the activity increase as well as spore formation occurred one day later, indicating that the induction of catalase activity during starvation was due to Cat2. In wt starved cells, catalase activity was not induced by H2O2. These results suggest that Cat2 is the primary housekeeping catalase during M. xanthus growth and starvation-induced development, whereas Cat1 may have a complementary role, being responsible for the rapid degradation of H2O2 in proliferating vegetative cells subjected to oxidative stress.

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Enzymatic characterization of five thioredoxins and a thioredoxin reductase from Myxococcus xanthus
Ryota Tanifuji, Yoshio Kimura
FEMS Microbiology Letters.2024;[Epub] CrossRef
Overexpression of cat2 restores antioxidant properties and production traits in degenerated strains of Volvariella volvacea
Jianing Zhu, Wenpei Wang, Wanhe Sun, Yuanxi Lei, Qiangfei Tan, Gahong Zhao, Jianmin Yun, Fengyun Zhao
Free Radical Biology and Medicine.2024; 215: 94. CrossRef
Alleviation of H2O2 toxicity by extracellular catalases in the phycosphere of Microcystis aeruginosa
Yerim Park, Wonjae Kim, Yeji Cha, Minkyung Kim, Woojun Park
Harmful Algae.2024; 137: 102680. CrossRef
Cis-3-Indoleacrylic Acid: A Nematicidal Compound from Streptomyces youssoufiensis YMF3.862 as V-ATPase Inhibitor on Meloidogyne incognita
Min Chen, Ying Huang, Li Ma, Jian-Jin Liu, Yi Cao, Pei-Ji Zhao, Ming-He Mo
Journal of Agricultural and Food Chemistry.2024; 72(44): 24347. CrossRef
Broad-spectrum ROS autonomous scavenging polysaccharide-based vehicle to improve the bioactivity of blueberry anthocyanidins through intestinal synergistic mucoadhesion
Jingwen Xu, Yue Zhang, Xiaolin Yao, Sijuan Wang, Guangwen Luo, Kaiqiang Lv, Yongkang Zhang, Guoliang Li
Food Hydrocolloids.2024; 152: 109899. CrossRef
Polyphosphate Plays a Significant Role in the Maturation of Spores in Myxococcus xanthus
Daiki Harita, Hiroka Matsukawa, Yoshio Kimura
Current Microbiology.2024;[Epub] CrossRef
Discovery of 2-Naphthol from the Leaves of Actephila merrilliana as a Natural Nematicide Candidate
Xi Zhang, Zhan Hu, Shuai Wang, Fengman Yin, Yuyang Wei, Jia Xie, Ranfeng Sun
Journal of Agricultural and Food Chemistry.2023; 71(36): 13209. CrossRef

Molecular characterization of Hsf1 as a master regulator of heat shock response in the thermotolerant methylotrophic yeast Ogataea parapolymorpha: Jin Ho Choo , Su-Bin Lee , Hye Yun Moon , Kun Hwa Lee , Su Jin Yoo , Keun Pil Kim , Hyun Ah Kang; J. Microbiol. 2021;59(2):151-163. Published online February 1, 2021; DOI: https://doi.org/10.1007/s12275-021-0646-2

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Abstract

Ogataea parapolymorpha (Hansenula polymorpha DL-1) is a thermotolerant methylotrophic yeast with biotechnological applications. Here, O. parapolymorpha genes whose expression is induced in response to heat shock were identified by transcriptome analysis and shown to possess heat shock elements (HSEs) in their promoters. The function of O. parapolymorpha HSF1 encoding a putative heat shock transcription factor 1 (OpHsf1) was characterized in the context of heat stress response. Despite exhibiting low sequence identity (26%) to its Saccharomyces cerevisiae homolog, OpHsf1 harbors conserved domains including a DNA binding domain (DBD), domains involved in trimerization (TRI), transcriptional activation (AR1, AR2), transcriptional repression (CE2), and a C-terminal modulator (CTM) domain. OpHSF1 could complement the temperature sensitive (Ts) phenotype of a S. cerevisiae hsf1 mutant. An O. parapolymorpha strain with an H221R mutation in the DBD domain of OpHsf1 exhibited significantly retarded growth and a Ts phenotype. Intriguingly, the expression of heat-shock-protein‒coding genes harboring HSEs was significantly decreased in the H221R mutant strain, even under non-stress conditions, indicating the importance of the DBD for the basal growth of O. parapolymorpha. Notably, even though the deletion of C-terminal domains (ΔCE2, ΔAR2, ΔCTM) of OpHsf1 destroyed complementation of the growth defect of the S. cerevisiae hsf1 strain, the C-terminal domains were shown to be dispensable in O. parapolymorpha. Overexpression of OpHsf1 in S. cerevisiae increased resistance to transient heat shock, supporting the idea that OpHsf1 could be useful in the development of heatshock‒ resistant yeast host strains.

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A comprehensive review and comparison of L-tryptophan biosynthesis in Saccharomyces cerevisiae and Escherichia coli
Xinru Ren, Yue Wei, Honglu Zhao, Juanjuan Shao, Fanli Zeng, Zhen Wang, Li Li
Frontiers in Bioengineering and Biotechnology.2023;[Epub] CrossRef
Heat shock in Cronobacter sakazakii induces direct protection and cross-protection against simulated gastric fluid stress
Hongmei Niu, MingzheYang, Yonghua Qi, Yangtai Liu, Xiang Wang, Qingli Dong
Food Microbiology.2022; 103: 103948. CrossRef
A review of yeast: High cell-density culture, molecular mechanisms of stress response and tolerance during fermentation
Dongxu Shen, Xiaoli He, Peifang Weng, Yanan Liu, Zufang Wu
FEMS Yeast Research.2022;[Epub] CrossRef

Development of a strategy for the screening of α-glucosidase-producing microorganisms: Bo Zhou+ , Nan Huang+ , Wei Zeng+ , Hao Zhang , Guiguang Chen , Zhiqun Liang; J. Microbiol. 2020;58(2):163-172. Published online January 29, 2020; DOI: https://doi.org/10.1007/s12275-020-9267-4

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Abstract

α-Glucosidase is a crucial enzyme for the production of isomaltooligosaccharide. In this study, a novel method comprising eosin Y (EY) and α-D-methylglucoside (AMG) in glass plates was tested for the primary screening of α-glucosidaseproducing strains. First, α-glucosidase-producing Aspergillus niger strains were selected on plates containing EY and AMG based on transparent zone formation resulting from the solubilization of EY by the hydrolyzed product. Conventional
methods
that use trypan blue (TB) and p-nitrophenyl-α-Dglucopyranoside (pPNP) as indicators were then compared with the new strategy. The results showed that EY-containing plates provide the advantages of low price and higher specificity for the screening of α-glucosidase-producing strains. We then evaluated the correlation between the hydrolytic activity of α-glucosidase and diffusion distance, and found that good linearity could be established within a 6–75 U/ml enzyme concentration range. Finally, the hydrolytic and transglycosylation activities of α-glucosidase obtained from the target isolates were determined by EY plate assay and 3,5- dinitrosalicylic acid-Saccharomyces cerevisiae assay, respectively. The results showed that the diameter of the transparent zone varied among isolates was positively correlated with α-glucosidase hydrolytic activity, while good linearity could also be established between α-glucosidase transglycosylation activity and non-fermentable reducing sugars content. With this strategy, 7 Aspergillus niger mutants with high yield of α-glucosidase from 200 obvious single colonies on the primary screen plate were obtained.

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Purification, characterization of a novel α-glucosidase from Debaryomyces hansenii strain MCC 0202 and chromatographic separation for high purity isomalto-oligosaccharides production
Saravanan Rengarajan, Rameshthangam Palanivel
Process Biochemistry.2024; 136: 109. CrossRef
Development of a PMA‐LAMP visual detection assay for viable Cronobacter sakazakii
Qiming Chen, Yang Yu, Xiaodi Chen, Fangming Tu, Peng Wang, Junyi Huang, Zhanmin Liu
International Journal of Dairy Technology.2024; 77(2): 427. CrossRef
Identification of chitin synthase activator in Aspergillus niger and its application in citric acid fermentation
Chunxu Jiang, Han Wang, Menghan Liu, Li Wang, Ruwen Yang, Peng Wang, Zongmei Lu, Yong Zhou, Zhiming Zheng, Genhai Zhao
Applied Microbiology and Biotechnology.2022; 106(21): 6993. CrossRef
Cloning and characterization of a recombinant α-glucosidase from Ensifer adhaerens NBRC 100388 and evaluation of its glucosyl transfer activity
Tatsuya Suzuki, Miyu Fukaya, Kazuki Takahashi, Michiki Takeuchi, Ryotaro Hara, Jun Ogawa, Makoto Ueda
Biocatalysis and Agricultural Biotechnology.2020; 30: 101837. CrossRef

IgG and IgM responses to human papillomavirus L1 virus-like particle as a function of dosing schedule and vaccine formulation: Min-Hye Park , Ji Won You , Hyoung Jin Kim , Hong-Jin Kim; J. Microbiol. 2019;57(9):821-827. Published online August 27, 2019; DOI: https://doi.org/10.1007/s12275-019-9308-z

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Abstract

Most commercialized virus-like particle (VLP) vaccines use aluminum salt as adjuvant, even though VLPs provoke adequate antibody responses without adjuvant. We do not have detailed knowledge of how adjuvant affects the profile of anti- VLP antibodies. Meanwhile, there is evidence that differences between vaccination protocols influence the glycosylation of antibodies, which may alter their effector functions. In the present study a murine model was used to investigate the effects of dosing schedule and adjuvant on the antibody profiles and glycosylation levels of antigen-specific antibody responses to human papillomavirus type 16 L1 (HPV16 L1) VLPs. Mice received subcutaneously 2,000 ng of antigen divided into 4 or 7 doses. The HPV16 L1 VLPs elicited > 4 log10 anti-HPV16 L1 IgG titers without adjuvant, and aluminum hydroxide as adjuvant increased IgG titers 1.3- to 4-fold and reduced the anti-HPV16 L1 IgG2a / anti-HPV16 L1 IgG1 ratio value (use of aluminum hydroxide reduced the ratio of the IgG2a). Immunization with HPV16 L1 VLPs in combination with Freund’s adjuvant enhanced IgG titers 5- to 12- fold. Seven-dose immunization markedly increased anti- HPV16 L1 IgM titers compared to four-dose immunization, as well as increasing the proportion of glycosylated antibodies. Our results suggest that antibody glycosylation can be controlled immunologically, and IgG and IgM profiles and glycosylation profiles of the vaccine-induced antibodies can be used as indicators reflecting the vaccine characteristics. These
results
indicate that the HPV16 L1 VLP dosing schedule can affect the quality of antigen-specific antibody responses. We suggest that dosing schedules should be noted in vaccination protocols for VLP-based vaccines.

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Human papillomavirus vaccines: organisation and experience of preclinical studies
A. S. Korovkin, T. N. Nikitina, T. Yu. Kozlova, D. V. Gorenkov, A. R. Volgin
Biological Products. Prevention, Diagnosis, Treatment.2024; 24(3): 243. CrossRef
Chimeric Hepatitis B core virus-like particles harboring SARS-CoV2 epitope elicit a humoral immune response in mice
Sima Sazegari, Malihe Akbarzadeh Niaki, Alireza Afsharifar, Ali Niazi, Abdollah Derakhshandeh, Maryam Moradi Vahdat, Farshad Hemmati, Mohammad Hadi Eskandari
Microbial Cell Factories.2023;[Epub] CrossRef
Anti-JMH alloantibody in inherited JMH-negative patients leads to immunogenic destruction of JMH-positive RBCs
Zhaohu Yuan, Yaming Wei, Xiaojie Chen, Shufei He, Kui Cai, Minglu Zhong, Huiying Huang, Xinxin Tong, Zhen Liu, Xuexin Yang
Clinical and Experimental Immunology.2021; 205(2): 182. CrossRef
Prevalence of antibodies against a cyclic peptide mimicking the FG loop of the human papillomavirus type 16 capsid among Tunisian women
Elham Hassen, Devendra Bansal, Randa Ghdira, Anouar Chaieb, Hedi Khairi, Abdelfattah Zakhama, Sami Remadi, Johan Hoebeke, Ali A. Sultan, Lotfi Chouchane
Journal of Translational Medicine.2020;[Epub] CrossRef

[PROTOCOL] Structural analysis of N-/O-glycans assembled on proteins in yeasts: Eun Jung Thak , Jungho Kim , Dong-Jik Lee , Jeong Yoon Kim , Hyun Ah Kang; J. Microbiol. 2018;56(1):11-23. Published online January 4, 2018; DOI: https://doi.org/10.1007/s12275-018-7468-x

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Abstract

Protein glycosylation, the most universal and diverse posttranslational modification, can affect protein secretion, stability, and immunogenicity. The structures of glycans attached to proteins are quite diverse among different organisms and even within yeast species. In yeast, protein glycosylation plays key roles in the quality control of secretory proteins, and particularly in maintaining cell wall integrity. Moreover, in pathogenic yeasts, glycans assembled on cell-surface glycoproteins can mediate their interactions with host cells. Thus, a comprehensive understanding of protein glycosylation in various yeast species and defining glycan structure characteristics can provide useful information for their biotechnological and clinical implications. Yeast-specific glycans are a target for glyco-engineering; implementing human-type glycosylation pathways in yeast can aid the production of recombinant glycoproteins with therapeutic potential. The virulenceassociated glycans of pathogenic yeasts could be exploited as novel targets for antifungal agents. Nowadays, several glycomics techniques facilitate the generation of species- and strain-specific glycome profiles and the delineation of modified glycan structures in mutant and engineered yeast cells. Here, we present the protocols employed in our laboratory to investigate the N- and O-glycan chains released from purified glycoproteins or cell wall mannoproteins in several yeast species.

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Song Yang, Jiao Sun, Aoran Xue, Guihua Li, Chenhao Sun, Jie Hou, Qing-Ming Qin, Mingzhe Zhang
Journal of Agricultural and Food Chemistry.2024; 72(34): 18824. CrossRef
Komagataella phaffii as a Platform for Heterologous Expression of Enzymes Used for Industry
Tamara M. Khlebodarova, Natalia V. Bogacheva, Andrey V. Zadorozhny, Alla V. Bryanskaya, Asya R. Vasilieva, Danil O. Chesnokov, Elena I. Pavlova, Sergey E. Peltek
Microorganisms.2024; 12(2): 346. CrossRef
Proteomic Analysis of Cell Wall Proteins with Various Linkages in Fusarium graminearum
Heeji Moon, Kyunghun Min, Jessica Winarto, Soobin Shin, Hosung Jeon, Dae-Geun Song, Hokyoung Son
Journal of Agricultural and Food Chemistry.2024; 72(11): 6028. CrossRef
Analysis of carbohydrates and glycoconjugates by matrix‐assisted laser desorption/ionization mass spectrometry: An update for 2017–2018
David J. Harvey
Mass Spectrometry Reviews.2023; 42(1): 227. CrossRef
Rna-Seq Based Transcriptomic Analysis of the Non-Conventional Yeast Spathaspora Passalidarum During Melle-Boinot Cell Recycle in Xylose-Glucose Mixtures
Thiago Neitzel, Cleilton Santos Lima, Eduardo Hafemann, Douglas Antonio Alvaredo Paixão, Joaquim Martins Junior, Gabriela Felix Persinoti, Leandro Vieira dos Santos, jaciane ienczak
SSRN Electronic Journal .2022;[Epub] CrossRef
RNA-seq based transcriptomic analysis of the non-conventional yeast Spathaspora passalidarum during Melle-boinot cell recycle in xylose-glucose mixtures
Thiago Neitzel, Cleilton Santos Lima, Eduardo Hafemann, Douglas Antonio Alvaredo Paixão, Joaquim Martins Junior, Gabriela Felix Persinoti, Leandro Vieira dos Santos, Jaciane Lutz Ienczak
Renewable Energy.2022; 201: 486. CrossRef
Pushing and pulling proteins into the yeast secretory pathway enhances recombinant protein secretion
Richard J. Zahrl, Roland Prielhofer, Özge Ata, Kristin Baumann, Diethard Mattanovich, Brigitte Gasser
Metabolic Engineering.2022; 74: 36. CrossRef
Extension of O -Linked Mannosylation in the Golgi Apparatus Is Critical for Cell Wall Integrity Signaling and Interaction with Host Cells in Cryptococcus neoformans Pathogenesis
Eun Jung Thak, Ye Ji Son, Dong-Jik Lee, Hyunah Kim, Jung Ho Kim, Su-Bin Lee, Yu-Byeong Jang, Yong-Sun Bahn, Connie B. Nichols, J. Andrew Alspaugh, Hyun Ah Kang, Michael Lorenz
mBio.2022;[Epub] CrossRef
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Ji-Yeon Kim, Woo Hong Joo, Dong-Soo Shin, Yong-Ill Lee, Chin Fen Teo, Jae-Min Lim
Analytical Biochemistry.2021; 621: 114152. CrossRef
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Jinkai Zang, Yuanfei Zhu, Yu Zhou, Chenjian Gu, Yufang Yi, Shuxia Wang, Shiqi Xu, Gaowei Hu, Shujuan Du, Yannan Yin, Yalei Wang, Yong Yang, Xueyang Zhang, Haikun Wang, Feifei Yin, Chao Zhang, Qiang Deng, Youhua Xie, Zhong Huang
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Marta Calatayud, Rosa Aragao Börner, Jonas Ghyselinck, Lynn Verstrepen, Jelle De Medts, Pieter Van den Abbeele, Claire L. Boulangé, Sarah Priour, Massimo Marzorati, Sami Damak
Nutrients.2021; 13(11): 3897. CrossRef
Genome-wide functional analysis of phosphatases in the pathogenic fungus Cryptococcus neoformans
Jae-Hyung Jin, Kyung-Tae Lee, Joohyeon Hong, Dongpil Lee, Eun-Ha Jang, Jin-Young Kim, Yeonseon Lee, Seung-Heon Lee, Yee-Seul So, Kwang-Woo Jung, Dong-Gi Lee, Eunji Jeong, Minjae Lee, Yu-Byeong Jang, Yeseul Choi, Myung Ha Lee, Ji-Seok Kim, Seong-Ryong Yu,
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David J. Harvey
Mass Spectrometry Reviews.2020; 39(5-6): 586. CrossRef
Yeast synthetic biology for designed cell factories producing secretory recombinant proteins
Eun Jung Thak, Su Jin Yoo, Hye Yun Moon, Hyun Ah Kang
FEMS Yeast Research.2020;[Epub] CrossRef
Core N -Glycan Structures Are Critical for the Pathogenicity of Cryptococcus neoformans by Modulating Host Cell Death
Eun Jung Thak, Su-Bin Lee, Shengjie Xu-Vanpala, Dong-Jik Lee, Seung-Yeon Chung, Yong-Sun Bahn, Doo-Byoung Oh, Mari L. Shinohara, Hyun Ah Kang, J. Andrew Alspaugh
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Tohru Ikegami
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Nidia Maldonado-Carmona, Melissa Vázquez-Hernández, Osiris Jair Patiño Chávez, Stefany Daniela Rodríguez-Luna, Omar Jiménez Rodríguez, Sergio Sanchez, Corina Diana Ceapă
Current Opinion in Pharmacology.2019; 48: 1. CrossRef

Functional analysis of recombinant human and Yarrowia lipolytica O-GlcNAc transferases expressed in Saccharomyces cerevisiae: Hye Ji Oh , Yun Moon , Seon Ah Cheon , Yoonsoo Hahn , Hyun Ah Kang; J. Microbiol. 2016;54(10):667-674. Published online September 30, 2016; DOI: https://doi.org/10.1007/s12275-016-6401-4

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Abstract

O-linked β-N-acetylglucosamine (O-GlcNAc) glycosylation is an important post-translational modification in many cellular processes. It is mediated by O-GlcNAc transferases (OGTs), which catalyze the addition of O-GlcNAc to serine or threonine residues of the target proteins. In this study, we expressed a putative Yarrowia lipolytica OGT (YlOGT), the only homolog identified in the subphylum Saccharomycotina through bioinformatics analysis, and the human OGT (hOGT) as recombinant proteins in Saccharomyces cerevisiae, and performed their functional characterization. Immunoblotting assays using antibody against O-GlcNAc revealed that recombinant hOGT (rhOGT), but not the recombinant YlOGT (rYlOGT), undergoes auto-O-GlcNAcylation in the heterologous host S. cerevisiae. Moreover, the rhOGT expressed in S. cerevisiae showed a catalytic activity during in vitro assays using casein kinase II substrates, whereas no such activity was obtained in rYlOGT. However, the chimeric human-Y. lipolytica OGT, carrying the human tetratricopeptide repeat (TPR) domain along with the Y. lipolytica catalytic domain (CTD), mediated the transfer of O-GlcNAc moiety during the in vitro assays. Although the overexpression of full-length OGTs inhibited the growth of S. cerevisiae, no such inhibition was obtained upon overexpression of only the CTD fragment, indicating the role of TPR domain in growth inhibition. This is the first report on the functional analysis of the fungal OGT, indicating that the Y. lipolytica OGT retains its catalytic activity, although the physiological role and substrates of YlOGT remain to be elucidated.

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GREB1: An evolutionarily conserved protein with a glycosyltransferase domain links ERα glycosylation and stability to cancer
Eun Myoung Shin, Vinh Thang Huynh, Sultan Abda Neja, Chia Yi Liu, Anandhkumar Raju, Kelly Tan, Nguan Soon Tan, Jayantha Gunaratne, Xuezhi Bi, Lakshminarayan M. Iyer, L. Aravind, Vinay Tergaonkar
Science Advances.2021;[Epub] CrossRef
Contribution of yeast models to virus research
R Sahaya Glingston, Jyoti Yadav, Jitika Rajpoot, Neha Joshi, Shirisha Nagotu
Applied Microbiology and Biotechnology.2021; 105(12): 4855. CrossRef
A Sweet Embrace: Control of Protein–Protein Interactions by O-Linked β-N-Acetylglucosamine
Heather J. Tarbet, Clifford A. Toleman, Michael Boyce
Biochemistry.2018; 57(1): 13. CrossRef

Research Support, Non-U.S. Gov't

Sublingual Administration of Bacteria-Expressed Influenza Virus Hemagglutinin 1 (HA1) Induces Protection against Infection with 2009 Pandemic H1N1 Influenza Virus: Byoung-Shik Shim , Jung-ah Choi , Ho-Hyun Song , Sung-Moo Park , In Su Cheon , Ji-Eun Jang , Sun Je Woo , Chung Hwan Cho , Min-Suk Song , Hyemi Kim , Kyung Joo Song , Jae Myun Lee , Suhng Wook Kim , Dae Sub Song , Young Ki Choi , Jae-Ouk Kim , Huan Huu Nguyen , Dong Wook Kim , Young Yil Bahk , Cheol-Heui Yun , Man Ki Song; J. Microbiol. 2013;51(1):130-135. Published online March 2, 2013; DOI: https://doi.org/10.1007/s12275-013-2399-z

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Abstract: Influenza viruses are respiratory pathogens that continue to pose a significantly high risk of morbidity and mortality of humans worldwide. Vaccination is one of the most effective strategies for minimizing damages by influenza outbreaks. In addition, rapid development and production of efficient vaccine with convenient administration is required in case of influenza pandemic. In this study, we generated recombinant influenza virus hemagglutinin protein 1 (sHA1) of 2009 pandemic influenza virus as a vaccine candidate using a wellestablished bacterial expression system and administered it into mice via sublingual (s.l.) route. We found that s.l. immunization with the recombinant sHA1 plus cholera toxin (CT) induced mucosal antibodies as well as systemic antibodies including neutralizing Abs and provided complete protection against infection with pandemic influenza virus A/CA/04/09 (H1N1) in mice. Indeed, the protection efficacy was comparable with that induced by intramuscular (i.m.) immunization route utilized as general administration route of influenza vaccine. These results suggest that s.l. vaccination with the recombinant non-glycosylated HA1 protein offers an alternative strategy to control influenza outbreaks including pandemics.

Journal Article

Characterization of Trichoderma reesei Endoglucanase II Expressed Heterologously in Pichia pastoris for Better Biofinishing and Biostoning: Sutanu Samanta , Asitava Basu , Umesh Chandra Halder , Soumitra Kumar Sen; J. Microbiol. 2012;50(3):518-525. Published online June 30, 2012; DOI: https://doi.org/10.1007/s12275-012-1207-5

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Abstract: The endoglucanase II of Trichoderma reesei is considered the most effective enzyme for biofinishing cotton fabrics and biostoning denim garments. However, the commercially available preparation of endoglucanase II is usually mixed with other cellulase components, especially endoglucanase I, resulting in hydrolysis and weight loss of garments during biofinishing and biostoning. We thus isolated the endoglucanase II gene from T. reesei to express this in Pichia pastoris, under the control of a methanol-inducible AOX1 promoter, to avoid the presence of other cellulase components. A highly expressible Mut+ transformant was selected and its expression in BMMH medium was found most suitable for the production of large amounts of the recombinant protein. Recombinant endoglucanase II was purified to electrophoretic homogeneity, and functionally characterized by activity staining. The specific activity of recombinant endoglucanase II was found to be 220.57 EU/mg of protein. Purified recombinant endoglucanase II was estimated to have a molecular mass of 52.8 kDa. The increase in molecular mass was likely due to hyperglycosylation. Hyperglycosylation of recombinant endoglucanase II secreted by P. pastoris did not change the temperature or pH optima as compared to the native protein, but did result in increased thermostability. Kinetic analysis showed that recombinant endoglucanase was most active against amorphous cellulose, such as carboxymethyl cellulose, for which it also had a high affinity.

Research Support, Non-U.S. Gov'ts

Purification and Characterization of the α-Glucosidase Produced by Thermophilic Fungus Thermoascus aurantiacus CBMAI 756: Ana Flávia Azevedo Carvalho , Maurício Boscolo , Roberto da Silva , Henrique Ferreira , Eleni Gomes; J. Microbiol. 2010;48(4):452-459. Published online August 20, 2010; DOI: https://doi.org/10.1007/s12275-010-9319-2

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Abstract: Αn α-glucosidase enzyme produced by the fungus Thermoascus aurantiacus CBMAI 756 was purified by ultra filtration, ammonium sulphate precipitation, and chromatography using Q Sepharose, Sephacryl S-200, and Superose 12 columns. The apparent molecular mass of the enzyme was 83 kDa as determined in gel electrophoresis. Maximum activity was observed at pH 4.5 at 70°C. Enzyme showed stability stable in the pH range of 3.0-9.0 and lost 40% of its initial activity at the temperatures of 40, 50, and 60°C. In the presence of ions Na+, Ba2+, Co2+, Ni2+, Mg2+, Mn2+, Al3+, Zn2+, Ca2+ this enzyme maintained 90-105% of its maximum activity and was inhibited by Cr3+, Ag+, and Hg2+. The enzyme showed a transglycosylation property, by the release of oligosaccharides after 3 h of incubation with maltose, and specificity for short maltooligosaccharides and α-PNPG. The Km measured for the α-glucosidase was 0.07 μM, with a Vmax of 318.0 μmol/min/mg.

Glycosylation and Production Characteristics of Epothilones in Alkali-Tolerant Sorangium cellulosum Strain So0157-2: Lin Zhao , Peng-fei Li , Chun-hua Lu , Shu-guang Li , Yue-mao Shen , Yue-zhong Li; J. Microbiol. 2010;48(4):438-444. Published online August 20, 2010; DOI: https://doi.org/10.1007/s12275-010-0048-3

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Abstract

3-O-α-D-ribofuranosyl epothilone A (epothiloneoside A) is a major component of glycosylated epothilones in Sorangium cellulosum strain So0157-2. The production and glycosylation ratios of epothiloneoside A in both solid and liquid culture conditions with various pH values and carbon sources were studied. The results showed that glycosylation occurs whenever epothilones are produced, regardless of changes in pH values, production time curves, and different carbon sources. We suggest that glycosylation is a stable process, paralleling the biosynthesis of epothilones in the So0157-2 strain.

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Genetic manipulation and tools in myxobacteria for the exploitation of secondary metabolism
Xinjing Yue, Duohong Sheng, Li Zhuo, Yue-Zhong Li
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Effect of Glycosylation on the Biochemical Properties of beta-Xylosidases from Aspergillus versicolor: Alexandre Favarin Somera , Marita Gimenez Pereira , Luis Henrique Souza Guimaraes , Maria de Lourdes Teixeira de Moraes Polizeli , Hector Francisco Terenzi , Rosa Prazeres Melo Furriel , Joao Atilio Jorge; J. Microbiol. 2009;47(3):270-276. Published online June 26, 2009; DOI: https://doi.org/10.1007/s12275-008-0286-9

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Abstract: Aspergillus versicolor grown on xylan or xylose produces two beta-xylosidases with differences in biochemical properties and degree of glycosylation. We investigated the alterations in the biochemical properties of these beta-xylosidases after deglycosylation with Endo-H or PNGase F. After deglycosylation, both enzymes migrated faster in PAGE or SDS-PAGE exhibiting the same Rf. Temperature optimum of xylan-induced and xylose-induced beta-xylosidases was 45oC and 40oC, respectively, and 35oC after deglycosylation. The xylan- induced enzyme was more active at acidic pH. After deglycosylation, both enzymes had the same pH optimum of 6.0. Thermal resistance at 55oC showed half-life of 15 min and 9 min for xylose- and xylan-induced enzymes, respectively. After deglycosylation, both enzymes exhibited half-lives of 7.5 min. Native enzymes exhibited different responses to ions, while deglycosylated enzymes exhibited identical responses. Limited proteolysis yielded similar polypeptide profiles for the deglycosylated enzymes, suggesting a common polypeptide core with differential glycosylation apparently responsible for their biochemical and biophysical differences.

Journal Article

Melanogenesis Inhibitory Effects of Methanolic Extracts of Umbilicaria esculenta and Usnea longissima: Moo-Sung Kim , Hong-Bum Cho; J. Microbiol. 2007;45(6):578-582.; DOI: https://doi.org/2605 [pii]

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Abstract: The primary objective of this study was to assess the in vitro melanogenesis inhibitory effects of methanolic extracts of the edible and medicinal lichens, Umbilicaria (Gyrophora) esculenta and Usnea longissima. The quantities of the total phenolic compounds of methanolic extract of the two lichen extracts were determined to be 1.46% and 2.62%, respectively. In order to evaluate the antioxidative effects of the extracts, we also measured electron donating abilities (EDA) and lipid peroxidation rates. The EDA values measured by the reduction of 1.1''-diphenyl-2-picrylhydrazyl (DPPH) were 72.8% and 80.7% for the extracts, with SC50 (median scavenging concentration) values of 1.29±0.05 mg/ml and 1.03±0.06 mg/ml, respectively. The rates of inhibition of lipid peroxidation using linoleic acid were 92.1% and 97.3% for the extracts, with IC50 (median inhibitory concentration) values of 0.57±0.05 mg/ml and 0.53±0.06 mg/ml, respectively. The inhibitory rates of the extracts against tyrosinase were 67.4% and 84.8%, respectively. The extracts were shown to reduce melanin formation in human melanoma cells. Melanin contents in the samples treated with 0.01% and 0.1% U. esculenta were 47.1% and 31.2%, respectively, and those treated with 0.01% and 0.1% Usnea longissima were 51.1% and 34.9%, respectively, whereas a value of 54.0% was registered when ascorbic acid was utilized as a positive control. In addition to direct tyrosinase inhibition, it was determined that the lichen extracts affected the activity of tyrosinase via the inhibition of tyrosinase glycosylation. As a result, the methanolic extracts of U. esculenta and Usnea longissima evidenced melanogenesis inhibitory effects, which occurred via multiple routes.

Research Support, Non-U.S. Gov'ts

Natural Iminosugar Derivatives of 1-Deoxynojirimycin Inhibit Glycosylation of Hepatitis Viral Envelope Proteins: James R. Jacob , Keith Mansfield , Jung Eun You , Bud C. Tennant , Young Ho Kim; J. Microbiol. 2007;45(5):431-440.; DOI: https://doi.org/2593 [pii]

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Abstract: A silkworm (Bombyx mori L.) extract known to contain naturally occurring iminosugars, including 1-deoxynojirimycin (1-DNJ) derived from the mulberry tree (Morus alba L.), was evaluated in surrogate HCV and HBV in vitro assays. Antiviral activity of the silkworm extract and one of its purified constituents, 1-DNJ, was demonstrated against bovine viral diarrhea virus (BVDV) and GB virus-B (GBV-B), both members of the Flaviviridae family, and against woodchuck hepatitis virus (WHV) and hepatitis B virus (HBV), both members of the Hepadnaviridae family of viruses. The silkworm extract exhibited a 1,300 fold greater antiviral effect against BVDV in comparison to purified 1-DNJ. Glycoprotein processing of BVDV envelope proteins was disrupted upon treatment with the naturally derived components. The glycosylation of the WHV envelope proteins was affected largely by treatment with the silkworm extract than with purified 1-DNJ as well. The mechanism of action for this therapy may lie in the generation of defective particles that are unable to initiate the next cycle of infection as demonstrated by inhibition of GBV-B in vitro. We postulate that the five constituent iminosugars present in the silkworm extract contribute, in a synergistic manner, toward the antiviral effects observed for the inhibition of intact maturation of hepatitis viral particles and may complement conventional therapies. These results indicate that pre-clinical testing of the natural silkworm extract with regards to the efficacy of treatment against viral hepatitis infections can be evaluated in the respective animal models, in preparation for clinical trials in humans.

Defining the N-Linked Glycosylation Site of Hantaan Virus Envelope Glycoproteins Essential for Cell Fusion: Feng Zheng , Lixian Ma , Lihua Shao , Gang Wang , Fengzhe Chen , Ying Zhang , Song Yang; J. Microbiol. 2007;45(1):41-47.; DOI: https://doi.org/2493 [pii]

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Abstract: The Hantaan virus (HTNV) is an enveloped virus that is capable of inducing low pH-dependent cell fusion. We molecularly cloned the viral glycoprotein (GP) and nucleocapsid (NP) cDNA of HTNV and expressed them in Vero E6 cells under the control of a CMV promoter. The viral gene expression was assessed using an indirect immunofluorescence assay and immunoprecipitation. The transfected Vero E6 cells expressing GPs, but not those expressing NP, fused and formed a syncytium following exposure to a low pH. Monoclonal antibodies (MAbs) against envelope GPs inhibited cell fusion, whereas MAbs against NP did not. We also investigated the N-linked glycosylation of HTNV GPs and its role in cell fusion. The envelope GPs of HTNV are modified by N-linked glycosylation at five sites: four sites on G1 (N134, N235, N347, and N399) and one site on G2 (N928). Site-directed mutagenesis was used to construct eight GP gene mutants, including five single N-glycosylation site mutants and three double-site mutants, which were then expressed in Vero E6 cells. The oligosaccharide chain on residue N928 of G2 was found to be crucial for cell fusion after exposure to a low pH. These results suggest that G2 is likely to be the fusion protein of HTNV.

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