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  1. Article ; Online: Characterization of intestinal O-glycome in reactive oxygen species deficiency.

    Saldova, Radka / Thomsson, Kristina A / Wilkinson, Hayden / Chatterjee, Maitrayee / Singh, Ashish K / Karlsson, Niclas G / Knaus, Ulla G

    PloS one

    2024  Volume 19, Issue 3, Page(s) e0297292

    Abstract: Inflammatory bowel disease (IBD) is characterized by chronic intestinal inflammation resulting from an inappropriate inflammatory response to intestinal microbes in a genetically susceptible host. Reactive oxygen species (ROS) generated by NADPH oxidases ...

    Abstract Inflammatory bowel disease (IBD) is characterized by chronic intestinal inflammation resulting from an inappropriate inflammatory response to intestinal microbes in a genetically susceptible host. Reactive oxygen species (ROS) generated by NADPH oxidases (NOX) provide antimicrobial defense, redox signaling and gut barrier maintenance. NADPH oxidase mutations have been identified in IBD patients, and mucus layer disruption, a critical aspect in IBD pathogenesis, was connected to NOX inactivation. To gain insight into ROS-dependent modification of epithelial glycosylation the colonic and ileal mucin O-glycome of mice with genetic NOX inactivation (Cyba mutant) was analyzed. O-glycans were released from purified murine mucins and analyzed by hydrophilic interaction ultra-performance liquid chromatography in combination with exoglycosidase digestion and mass spectrometry. We identified five novel glycans in ileum and found minor changes in O-glycans in the colon and ileum of Cyba mutant mice. Changes included an increase in glycans with terminal HexNAc and in core 2 glycans with Fuc-Gal- on C3 branch, and a decrease in core 3 glycans in the colon, while the ileum showed increased sialylation and a decrease in sulfated glycans. Our data suggest that NADPH oxidase activity alters the intestinal mucin O-glycans that may contribute to intestinal dysbiosis and chronic inflammation.
    MeSH term(s) Humans ; Mice ; Animals ; Reactive Oxygen Species ; Mucins/chemistry ; Inflammation ; Polysaccharides/chemistry ; Inflammatory Bowel Diseases ; NADPH Oxidases/genetics ; Intestinal Mucosa/chemistry
    Chemical Substances Reactive Oxygen Species ; Mucins ; Polysaccharides ; NADPH Oxidases (EC 1.6.3.-)
    Language English
    Publishing date 2024-03-14
    Publishing country United States
    Document type Journal Article
    ZDB-ID 2267670-3
    ISSN 1932-6203 ; 1932-6203
    ISSN (online) 1932-6203
    ISSN 1932-6203
    DOI 10.1371/journal.pone.0297292
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Defensive Properties of Mucin Glycoproteins during Respiratory Infections-Relevance for SARS-CoV-2.

    Chatterjee, Maitrayee / van Putten, Jos P M / Strijbis, Karin

    mBio

    2020  Volume 11, Issue 6

    Abstract: Mucus plays a pivotal role in protecting the respiratory tract against microbial infections. It acts as a primary contact site to entrap microbes and facilitates their removal from the respiratory tract via the coordinated beating of motile cilia. The ... ...

    Abstract Mucus plays a pivotal role in protecting the respiratory tract against microbial infections. It acts as a primary contact site to entrap microbes and facilitates their removal from the respiratory tract via the coordinated beating of motile cilia. The major components of airway mucus are heavily
    MeSH term(s) Bacterial Infections/metabolism ; COVID-19/virology ; Glycoproteins/metabolism ; Glycosylation ; Humans ; Mucin 5AC/metabolism ; Mucin-1/metabolism ; Mucin-5B/metabolism ; Mucins/metabolism ; Respiratory Tract Infections/microbiology ; Respiratory Tract Infections/prevention & control ; Respiratory Tract Infections/virology ; SARS-CoV-2/pathogenicity ; Virus Diseases/metabolism
    Chemical Substances Glycoproteins ; MUC1 protein, human ; MUC5AC protein, human ; MUC5B protein, human ; Mucin 5AC ; Mucin-1 ; Mucin-5B ; Mucins
    Keywords covid19
    Language English
    Publishing date 2020-11-12
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 2557172-2
    ISSN 2150-7511 ; 2161-2129
    ISSN (online) 2150-7511
    ISSN 2161-2129
    DOI 10.1128/mBio.02374-20
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: Glycosylated extracellular mucin domains protect against SARS-CoV-2 infection at the respiratory surface.

    Chatterjee, Maitrayee / Huang, Liane Z X / Mykytyn, Anna Z / Wang, Chunyan / Lamers, Mart M / Westendorp, Bart / Wubbolts, Richard W / van Putten, Jos P M / Bosch, Berend-Jan / Haagmans, Bart L / Strijbis, Karin

    PLoS pathogens

    2023  Volume 19, Issue 8, Page(s) e1011571

    Abstract: Mucins play an essential role in protecting the respiratory tract against microbial infections while also acting as binding sites for bacterial and viral adhesins. The heavily O-glycosylated gel-forming mucins MUC5AC and MUC5B eliminate pathogens by ... ...

    Abstract Mucins play an essential role in protecting the respiratory tract against microbial infections while also acting as binding sites for bacterial and viral adhesins. The heavily O-glycosylated gel-forming mucins MUC5AC and MUC5B eliminate pathogens by mucociliary clearance. Transmembrane mucins MUC1, MUC4, and MUC16 can restrict microbial invasion at the apical surface of the epithelium. In this study, we determined the impact of host mucins and mucin glycans on epithelial entry of SARS-CoV-2. Human lung epithelial Calu-3 cells express the SARS-CoV-2 entry receptor ACE2 and high levels of glycosylated MUC1, but not MUC4 and MUC16, on their cell surface. The O-glycan-specific mucinase StcE specifically removed the glycosylated part of the MUC1 extracellular domain while leaving the underlying SEA domain and cytoplasmic tail intact. StcE treatment of Calu-3 cells significantly enhanced infection with SARS-CoV-2 pseudovirus and authentic virus, while removal of terminal mucin glycans sialic acid and fucose from the epithelial surface did not impact viral entry. In Calu-3 cells, the transmembrane mucin MUC1 and ACE2 are located to the apical surface in close proximity and StcE treatment results in enhanced binding of purified spike protein. Both MUC1 and MUC16 are expressed on the surface of human organoid-derived air-liquid interface (ALI) differentiated airway cultures and StcE treatment led to mucin removal and increased levels of SARS-CoV-2 replication. In these cultures, MUC1 was highly expressed in non-ciliated cells while MUC16 was enriched in goblet cells. In conclusion, the glycosylated extracellular domains of different transmembrane mucins might have similar protective functions in different respiratory cell types by restricting SARS-CoV-2 binding and entry.
    MeSH term(s) Humans ; Mucins/metabolism ; Angiotensin-Converting Enzyme 2 ; COVID-19 ; SARS-CoV-2/metabolism ; CA-125 Antigen/metabolism ; Lung/metabolism ; Polysaccharides
    Chemical Substances Mucins ; Angiotensin-Converting Enzyme 2 (EC 3.4.17.23) ; CA-125 Antigen ; Polysaccharides
    Language English
    Publishing date 2023-08-10
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2205412-1
    ISSN 1553-7374 ; 1553-7374
    ISSN (online) 1553-7374
    ISSN 1553-7374
    DOI 10.1371/journal.ppat.1011571
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article ; Online: Glycosylated extracellular mucin domains protect against SARS-CoV-2 infection at the respiratory surface.

    Maitrayee Chatterjee / Liane Z X Huang / Anna Z Mykytyn / Chunyan Wang / Mart M Lamers / Bart Westendorp / Richard W Wubbolts / Jos P M van Putten / Berend-Jan Bosch / Bart L Haagmans / Karin Strijbis

    PLoS Pathogens, Vol 19, Iss 8, p e

    2023  Volume 1011571

    Abstract: Mucins play an essential role in protecting the respiratory tract against microbial infections while also acting as binding sites for bacterial and viral adhesins. The heavily O-glycosylated gel-forming mucins MUC5AC and MUC5B eliminate pathogens by ... ...

    Abstract Mucins play an essential role in protecting the respiratory tract against microbial infections while also acting as binding sites for bacterial and viral adhesins. The heavily O-glycosylated gel-forming mucins MUC5AC and MUC5B eliminate pathogens by mucociliary clearance. Transmembrane mucins MUC1, MUC4, and MUC16 can restrict microbial invasion at the apical surface of the epithelium. In this study, we determined the impact of host mucins and mucin glycans on epithelial entry of SARS-CoV-2. Human lung epithelial Calu-3 cells express the SARS-CoV-2 entry receptor ACE2 and high levels of glycosylated MUC1, but not MUC4 and MUC16, on their cell surface. The O-glycan-specific mucinase StcE specifically removed the glycosylated part of the MUC1 extracellular domain while leaving the underlying SEA domain and cytoplasmic tail intact. StcE treatment of Calu-3 cells significantly enhanced infection with SARS-CoV-2 pseudovirus and authentic virus, while removal of terminal mucin glycans sialic acid and fucose from the epithelial surface did not impact viral entry. In Calu-3 cells, the transmembrane mucin MUC1 and ACE2 are located to the apical surface in close proximity and StcE treatment results in enhanced binding of purified spike protein. Both MUC1 and MUC16 are expressed on the surface of human organoid-derived air-liquid interface (ALI) differentiated airway cultures and StcE treatment led to mucin removal and increased levels of SARS-CoV-2 replication. In these cultures, MUC1 was highly expressed in non-ciliated cells while MUC16 was enriched in goblet cells. In conclusion, the glycosylated extracellular domains of different transmembrane mucins might have similar protective functions in different respiratory cell types by restricting SARS-CoV-2 binding and entry.
    Keywords Immunologic diseases. Allergy ; RC581-607 ; Biology (General) ; QH301-705.5
    Subject code 570
    Language English
    Publishing date 2023-08-01T00:00:00Z
    Publisher Public Library of Science (PLoS)
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  5. Article ; Online: Phytochemical composition analysis and evaluation of

    Ghosh, Pranabesh / Das, Chandrima / Biswas, Swagata / Nag, Sudip Kumar / Dutta, Alolika / Biswas, Maitrayee / Sil, Sayantan / Hazra, Labani / Ghosh, Chandreyi / Das, Shaktijit / Saha, Moumita / Mondal, Nasim / Mandal, Suprodip / Ghosh, Anirban / Karmakar, Srabani / Chatterjee, Sirshendu

    F1000Research

    2020  Volume 9, Page(s) 493

    Abstract: Background: ...

    Abstract Background:
    MeSH term(s) Antioxidants/pharmacology ; Asteraceae/chemistry ; Cells, Cultured ; Cleome/chemistry ; Commelina/chemistry ; Euphorbia/chemistry ; Heliotropium/chemistry ; Humans ; India ; Leukocytes, Mononuclear/drug effects ; Phytochemicals/pharmacology ; Plant Extracts/pharmacology ; Plant Weeds/chemistry
    Chemical Substances Antioxidants ; Phytochemicals ; Plant Extracts
    Language English
    Publishing date 2020-06-02
    Publishing country England
    Document type Journal Article
    ZDB-ID 2699932-8
    ISSN 2046-1402 ; 2046-1402
    ISSN (online) 2046-1402
    ISSN 2046-1402
    DOI 10.12688/f1000research.22966.1
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  6. Article ; Online: Understanding the adhesion mechanism of a mucin binding domain from Lactobacillus fermentum and its role in enteropathogen exclusion.

    Chatterjee, Maitrayee / Pushkaran, Anju Choorakottayil / Vasudevan, Anil Kumar / Menon, Krishna Kumar N / Biswas, Raja / Mohan, Chethampadi Gopi

    International journal of biological macromolecules

    2017  Volume 110, Page(s) 598–607

    Abstract: Lactobacillus species possesses surface exposed Mucin Binding Protein (MucBP) which plays a role in adhesion to gastrointestinal mucin. MucBP contains one or more mucin binding domain (MBD), the functionality of which has yet not been characterized ... ...

    Abstract Lactobacillus species possesses surface exposed Mucin Binding Protein (MucBP) which plays a role in adhesion to gastrointestinal mucin. MucBP contains one or more mucin binding domain (MBD), the functionality of which has yet not been characterized thoroughly. Here, we have characterized a 93-amino acid MBD (MBD
    MeSH term(s) Adhesins, Bacterial/chemistry ; Adhesins, Bacterial/genetics ; Adhesins, Bacterial/metabolism ; Adhesins, Bacterial/pharmacology ; Animals ; Bacterial Adhesion/drug effects ; Enteropathogenic Escherichia coli/metabolism ; Enteropathogenic Escherichia coli/pathogenicity ; Lactobacillus fermentum/chemistry ; Lactobacillus fermentum/genetics ; Lactobacillus fermentum/metabolism ; Mucins/metabolism ; Protein Domains ; Proteus vulgaris/metabolism ; Proteus vulgaris/pathogenicity ; Salmonella paratyphi A/metabolism ; Salmonella paratyphi A/pathogenicity ; Shigella sonnei/metabolism ; Shigella sonnei/pathogenicity ; Swine
    Chemical Substances Adhesins, Bacterial ; Mucins
    Language English
    Publishing date 2017-10-20
    Publishing country Netherlands
    Document type Journal Article
    ZDB-ID 282732-3
    ISSN 1879-0003 ; 0141-8130
    ISSN (online) 1879-0003
    ISSN 0141-8130
    DOI 10.1016/j.ijbiomac.2017.10.107
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  7. Article: Understanding the adhesion mechanism of a mucin binding domain from Lactobacillus fermentum and its role in enteropathogen exclusion

    Chatterjee, Maitrayee / Anil Kumar Vasudevan / Anju Choorakottayil Pushkaran / Chethampadi Gopi Mohan / Krishna Kumar N. Menon / Raja Biswas

    International journal of biological macromolecules. 2017,

    2017  

    Abstract: Lactobacillus species possesses surface exposed Mucin Binding Protein (MucBP) which plays a role in adhesion to gastrointestinal mucin. MucBP contains one or more mucin binding domain (MBD), the functionality of which has yet not been characterized ... ...

    Abstract Lactobacillus species possesses surface exposed Mucin Binding Protein (MucBP) which plays a role in adhesion to gastrointestinal mucin. MucBP contains one or more mucin binding domain (MBD), the functionality of which has yet not been characterized thoroughly. Here, we have characterized a 93-amino acid MBD (MBD93) of MucBP (LAF_0673) from Lactobacillus fermentum. Multiple sequence alignment of L. fermentum MBD93 exhibited ∼60% sequence homology with MBDs from other Lactobacillus species. Further, we cloned, expressed and purified MBD93 from Escherichia coli as N-terminal histidine-tagged protein (6X His-MBD93). The purified MBD93 was able to bind to mucin and showed strong affinity towards the terminally expressed mucin glycans viz. N-acetylgalactosamine (GalNAc), N-acetylglucosamine (GlcNAc), Galactose (Gal), and Sialic acid (N-acetylneuraminic acid; Neu5Ac). In silico experiments further confirmed the interaction between homology modeled MBD93 to mucin glycans through hydrogen-bonding with its surface amino acid residues Ser57, Pro58, Ile60, Tyr63 and Ala65. We also have demonstrated that MBD93 was able to inhibit the adhesion of enteric pathogens, including E. coli, Salmonella Paratyphi A, Shigella sonnei and Proteus vulgaris to mucin. Our results suggested that L. fermentum MBD93 is a functionally sufficient unit to act as an adhesin and to protect from invading enteric pathogens.
    Keywords adhesins ; adhesion ; amino acids ; binding proteins ; enteropathogens ; Escherichia coli ; galactose ; gastrointestinal system ; hydrogen bonding ; Lactobacillus fermentum ; mucins ; N-acetylglucosamine ; polysaccharides ; Proteus vulgaris ; Salmonella Paratyphi A ; sequence alignment ; sequence homology ; Shigella sonnei ; sialic acid
    Language English
    Size p. .
    Publishing place Elsevier B.V.
    Document type Article
    Note Pre-press version
    ZDB-ID 282732-3
    ISSN 1879-0003 ; 0141-8130
    ISSN (online) 1879-0003
    ISSN 0141-8130
    DOI 10.1016/j.ijbiomac.2017.10.107
    Database NAL-Catalogue (AGRICOLA)

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  8. Article ; Online: Phytochemical composition analysis and evaluation of in vitro medicinal properties and cytotoxicity of five wild weeds

    Pranabesh Ghosh / Chandrima Das / Swagata Biswas / Sudip Kumar Nag / Alolika Dutta / Maitrayee Biswas / Sayantan Sil / Labani Hazra / Chandreyi Ghosh / Shaktijit Das / Moumita Saha / Nasim Mondal / Suprodip Mandal / Anirban Ghosh / Srabani Karmakar / Sirshendu Chatterjee

    F1000Research, Vol

    A comparative study [version 1; peer review: 1 approved, 2 approved with reservations]

    2020  Volume 9

    Abstract: Background: Medicinal plants are a source of phytochemicals and they are used for the treatment of several oxidative stress-related or other diseases for their effectiveness, low toxicity and easy availability. Five traditionally used and less ... ...

    Abstract Background: Medicinal plants are a source of phytochemicals and they are used for the treatment of several oxidative stress-related or other diseases for their effectiveness, low toxicity and easy availability. Five traditionally used and less characterized herbaceous weeds of West Bengal, India, namely, Heliotropium indicum, Tridax procumbens, Cleome rutidosperma, Commelina benghalensis and Euphorbia hirta, were investigated for the current research study. Methods: Aqueous and 70% ethanolic extracts of the leaves were analyzed for estimation of essential phytochemicals and to evaluate their in vitro antioxidant status, medicinal properties and cytotoxic effects. To the best of our knowledge, several assays and comparative evaluations using these herbs are reported for the first time. For quantitative study, UV-vis spectrophotometry and high-performance liquid chromatography with diode array detector HPLC-DAD techniques were used. Antibacterial properties were investigated using the Kirby-Bauer disc diffusion method. For in vitro anti-lithiatic study, a titration method was used. The cell viability assay was done using peripheral blood mononuclear cells. Results: The aqueous extract exhibits higher content of polyphenols, flavonoids, tannins and inhibition percentage values for free radical scavenging assays, whereas the 70% ethanolic extract exhibits higher content of alkaloids and cardiac glycosides. HPLC-DAD analysis of 70% ethanolic extracts led us to identify 10 predominant phenolic constituents. Euphorbia hirta extracts showed minimum cytotoxicity (cell death ~2.5% and 4% in water and 70% ethanolic extract, respectively), whereas Cleome rutidosperma and Tridax procumbens’ 70% ethanolic extracts showed higher cell death (~13% and 28%, respectively), compared with the control (cell death ~10-12%). Conclusions: The study concluded that of all the medicinal weeds selected for the current study, Euphorbia hirta possesses the highest amount of bioactive compounds and hence exhibits the highest in vitro antioxidant activity and promising in vitro medicinal properties.
    Keywords Medicine ; R ; Science ; Q
    Language English
    Publishing date 2020-06-01T00:00:00Z
    Publisher F1000 Research Ltd
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  9. Article ; Online: Antibiotic resistance in Pseudomonas aeruginosa and alternative therapeutic options.

    Chatterjee, Maitrayee / Anju, C P / Biswas, Lalitha / Anil Kumar, V / Gopi Mohan, C / Biswas, Raja

    International journal of medical microbiology : IJMM

    2016  Volume 306, Issue 1, Page(s) 48–58

    Abstract: Pseudomonas aeruginosa is a leading cause of nosocomial infections and is responsible for ∼10% of all hospital-acquired infections worldwide. It continues to pose a therapeutic challenge because of the high rate of morbidity and mortality associated with ...

    Abstract Pseudomonas aeruginosa is a leading cause of nosocomial infections and is responsible for ∼10% of all hospital-acquired infections worldwide. It continues to pose a therapeutic challenge because of the high rate of morbidity and mortality associated with it and the possibility of development of drug resistance during therapy. Standard antibiotic regimes against P. aeruginosa are increasingly becoming ineffective due to the rise in drug resistance. With the scope for developing new antibiotics being limited, alternative treatment options are gaining more and more attention. A number of recent studies reported complementary and alternative treatment options to combat P. aeruginosa infections. Quorum sensing inhibitors, phages, probiotics, anti-microbial peptides, vaccine antigens and antimicrobial nanoparticles have the potential to act against drug resistant strains. Unfortunately, most studies considering alternative treatment options are still confined in the pre-clinical stages, although some of these findings have tremendous potential to be turned into valuable therapeutics. This review is intended to raise awareness of several novel approaches that can be considered further for combating drug resistant P. aeruginosa infections.
    MeSH term(s) Biological Products/pharmacology ; Biological Products/therapeutic use ; Biological Therapy/methods ; Drug Resistance, Bacterial ; Humans ; Pseudomonas Infections/microbiology ; Pseudomonas Infections/therapy ; Pseudomonas aeruginosa/drug effects
    Chemical Substances Biological Products
    Language English
    Publishing date 2016-01
    Publishing country Germany
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 2006518-8
    ISSN 1618-0607 ; 1438-4221
    ISSN (online) 1618-0607
    ISSN 1438-4221
    DOI 10.1016/j.ijmm.2015.11.004
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  10. Article ; Online: Antimicrobial activity of plumbagin, a naturally occurring naphthoquinone from Plumbago rosea, against Staphylococcus aureus and Candida albicans.

    Nair, Sweatha V / Baranwal, Gaurav / Chatterjee, Maitrayee / Sachu, Arun / Vasudevan, Anil Kumar / Bose, Chinchu / Banerji, Asoke / Biswas, Raja

    International journal of medical microbiology : IJMM

    2016  Volume 306, Issue 4, Page(s) 237–248

    Abstract: Candida albicans and Staphylococcus aureus are opportunistic pathogens. Despite causing a number of independent infections, both pathogens can co-infect to cause urinary tract infections, skin infections, biofilm associated infections, sepsis and ... ...

    Abstract Candida albicans and Staphylococcus aureus are opportunistic pathogens. Despite causing a number of independent infections, both pathogens can co-infect to cause urinary tract infections, skin infections, biofilm associated infections, sepsis and pneumonia. Infections of these two pathogens especially their biofilm associated infections are often difficult to treat using currently available anti-bacterial and anti-fungal agents. In order to identify a common anti-microbial agent which could confer a broad range of protection against their infections, we screened several phytochemicals and identified plumbagin (5-hydroxy-2-methyl-1,4-naphthoquinone), a phytochemical from Plumbago species as a potent antimicrobial agent against S. aureus and C. albicans, with a minimum inhibitory concentration of 5μg/ml. Antimicrobial activity of plumbagin was validated using an ex-vivo porcine skin model. For better understanding of the antimicrobial activity of plumbagin, a Drosophila melanogaster infection model was used, where D. melanogaster was infected using S. aureus and C. albicans, or with both organisms. The fly's survival rate was dramatically increased when infected flies were treated using plumbagin. Further, plumbagin was effective in preventing and dispersing catheter associated biofilms formed by these pathogens. The overall results of this work provides evidence that plumbagin, possesses an excellent antimicrobial activity which should be explored further for the treatment of S. aureus and C. albicans infections.
    MeSH term(s) Animals ; Anti-Infective Agents/chemistry ; Anti-Infective Agents/isolation & purification ; Anti-Infective Agents/pharmacology ; Biofilms/drug effects ; Candida albicans/drug effects ; Candida albicans/physiology ; Candidiasis/drug therapy ; Disease Models, Animal ; Drosophila melanogaster ; Female ; Microbial Sensitivity Tests ; Naphthoquinones/chemistry ; Naphthoquinones/isolation & purification ; Naphthoquinones/pharmacology ; Phytochemicals/chemistry ; Phytochemicals/isolation & purification ; Phytochemicals/pharmacology ; Plumbaginaceae/chemistry ; Staphylococcal Infections/drug therapy ; Staphylococcus aureus/drug effects ; Staphylococcus aureus/physiology ; Survival Analysis ; Treatment Outcome
    Chemical Substances Anti-Infective Agents ; Naphthoquinones ; Phytochemicals ; plumbagin (YAS4TBQ4OQ)
    Language English
    Publishing date 2016-06
    Publishing country Germany
    Document type Journal Article
    ZDB-ID 2006518-8
    ISSN 1618-0607 ; 1438-4221
    ISSN (online) 1618-0607
    ISSN 1438-4221
    DOI 10.1016/j.ijmm.2016.05.004
    Database MEDical Literature Analysis and Retrieval System OnLINE

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