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Article ; Online: A proteome-wide screen to identify transcription factors interacting with the Vibrio cholerae rpoS promoter.

Ayala, Julio C / Benitez, Jorge A / Silva, Anisia J

2019 Volume 165, Page(s) 105702

Abstract: We describe a proteomic approach to identify transcription factors binding to a target promoter. The method's usefulness was tested by identifying proteins binding to the Vibrio cholerae rpoS promoter in response to cell density. Proteins identified in ... ...

Abstract	We describe a proteomic approach to identify transcription factors binding to a target promoter. The method's usefulness was tested by identifying proteins binding to the Vibrio cholerae rpoS promoter in response to cell density. Proteins identified in this screen included the nucleoid-associated protein Fis and the quorum sensing regulator HapR.
MeSH term(s)	Bacterial Proteins/genetics ; Gene Expression Regulation, Bacterial ; Promoter Regions, Genetic ; Proteome/metabolism ; Quorum Sensing ; Sigma Factor/genetics ; Transcription Factors/genetics ; Transcription, Genetic ; Vibrio cholerae/genetics
Chemical Substances	Bacterial Proteins ; Proteome ; Sigma Factor ; Transcription Factors ; sigma factor KatF protein, Bacteria
Language	English
Publishing date	2019-08-24
Publishing country	Netherlands
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	604916-3
ISSN	1872-8359 ; 0167-7012
ISSN (online)	1872-8359
ISSN	0167-7012
DOI	10.1016/j.mimet.2019.105702
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Zs.A 1849: Show issues

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Article ; Online: Chromatin Immunoprecipitation.

Ayala, Julio C / Benitez, Jorge A / Silva, Anisia J

Methods in molecular biology (Clifton, N.J.)

2018 Volume 1839, Page(s) 65–75

Abstract: Chromatin immunoprecipitation (ChIP) measures the physical association between a protein and DNA in the cell. In combination with next-generation sequencing, the technique enables the identification of DNA targets for the corresponding protein across an ... ...

Abstract	Chromatin immunoprecipitation (ChIP) measures the physical association between a protein and DNA in the cell. In combination with next-generation sequencing, the technique enables the identification of DNA targets for the corresponding protein across an entire genome. Here we describe the immunoprecipitation of Vibrio cholerae DNA bound to the histone-like nucleoid structuring protein (H-NS) tagged with the Flag epitope. The quality of the DNA obtained in this protocol is suitable for next-generation sequencing. The procedure described herein can be readily adapted to other bacteria and DNA-binding proteins.
MeSH term(s)	Bacterial Proteins/metabolism ; Chromatin Immunoprecipitation ; DNA-Binding Proteins ; High-Throughput Nucleotide Sequencing ; Protein Binding ; Real-Time Polymerase Chain Reaction ; Vibrio cholerae/genetics ; Vibrio cholerae/metabolism
Chemical Substances	Bacterial Proteins ; DNA-Binding Proteins
Language	English
Publishing date	2018-07-25
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ISSN	1940-6029
ISSN (online)	1940-6029
DOI	10.1007/978-1-4939-8685-9_7
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Article ; Online: Vibrio cholerae Biofilms and Cholera Pathogenesis.

Silva, Anisia J / Benitez, Jorge A

PLoS neglected tropical diseases

2016 Volume 10, Issue 2, Page(s) e0004330

Abstract: Vibrio cholerae can switch between motile and biofilm lifestyles. The last decades have been marked by a remarkable increase in our knowledge of the structure, regulation, and function of biofilms formed under laboratory conditions. Evidence has grown ... ...

Abstract	Vibrio cholerae can switch between motile and biofilm lifestyles. The last decades have been marked by a remarkable increase in our knowledge of the structure, regulation, and function of biofilms formed under laboratory conditions. Evidence has grown suggesting that V. cholerae can form biofilm-like aggregates during infection that could play a critical role in pathogenesis and disease transmission. However, the structure and regulation of biofilms formed during infection, as well as their role in intestinal colonization and virulence, remains poorly understood. Here, we review (i) the evidence for biofilm formation during infection, (ii) the coordinate regulation of biofilm and virulence gene expression, and (iii) the host signals that favor V. cholerae transitions between alternative lifestyles during intestinal colonization, and (iv) we discuss a model for the role of V. cholerae biofilms in pathogenicity.
MeSH term(s)	Biofilms/growth & development ; Cholera/microbiology ; Gastrointestinal Tract/microbiology ; Humans ; Vibrio cholerae/physiology ; Virulence ; Virulence Factors/biosynthesis
Chemical Substances	Virulence Factors
Language	English
Publishing date	2016-02-04
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Review
ZDB-ID	2429704-5
ISSN	1935-2735 ; 1935-2727
ISSN (online)	1935-2735
ISSN	1935-2727
DOI	10.1371/journal.pntd.0004330
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Article ; Online: Vibrio cholerae hemagglutinin(HA)/protease: An extracellular metalloprotease with multiple pathogenic activities.

Benitez, Jorge A / Silva, Anisia J

Toxicon : official journal of the International Society on Toxinology

2016 Volume 115, Page(s) 55–62

Abstract: Vibrio cholerae of serogroup O1 and O139, the etiological agent of the diarrheal disease cholera, expresses the extracellular Zn-dependent metalloprotease hemagglutinin (HA)/protease also reported as vibriolysin. This enzyme is also produced by non-O1/ ... ...

Abstract	Vibrio cholerae of serogroup O1 and O139, the etiological agent of the diarrheal disease cholera, expresses the extracellular Zn-dependent metalloprotease hemagglutinin (HA)/protease also reported as vibriolysin. This enzyme is also produced by non-O1/O139 (non-cholera) strains that cause mild, sporadic illness (i.e. gastroenteritis, wound or ear infections). Orthologs of HA/protease are present in other members of the Vibrionaceae family pathogenic to humans and fish. HA/protease belongs to the M4 neutral peptidase family and displays significant amino acid sequence homology to Pseudomonas aeruginosa elastase (LasB) and Bacillus thermoproteolyticus thermolysin. It exhibits a broad range of potentially pathogenic activities in cell culture and animal models. These activities range from the covalent modification of other toxins, the degradation of the protective mucus barrier and disruption of intestinal tight junctions. Here we review (i) the structure and regulation of HA/protease expression, (ii) its interaction with other toxins and the intestinal mucosa and (iii) discuss the possible role(s) of HA/protease in the pathogenesis of cholera.
MeSH term(s)	Amino Acid Sequence ; Animals ; Bacterial Proteins/chemistry ; Cholera/microbiology ; Humans ; Intestinal Mucosa/cytology ; Intestinal Mucosa/drug effects ; Metalloendopeptidases/chemistry ; Models, Animal ; Sequence Homology, Amino Acid ; Thermolysin/chemistry ; Vibrio cholerae/enzymology ; Vibrio cholerae/genetics
Chemical Substances	Bacterial Proteins ; Metalloendopeptidases (EC 3.4.24.-) ; hemagglutinin-protease (EC 3.4.24.-) ; vibriolysin protein, Vibrio proteolyticus (EC 3.4.24.25) ; pseudolysin, Pseudomonas aeruginosa (EC 3.4.24.26) ; Thermolysin (EC 3.4.24.27)
Language	English
Publishing date	2016-03-04
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Review
ZDB-ID	204479-1
ISSN	1879-3150 ; 0041-0101
ISSN (online)	1879-3150
ISSN	0041-0101
DOI	10.1016/j.toxicon.2016.03.003
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Zs.A 501: Show issues

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Article ; Online: H-NS: an overarching regulator of the Vibrio cholerae life cycle.

Ayala, Julio C / Silva, Anisia J / Benitez, Jorge A

Research in microbiology

2017 Volume 168, Issue 1, Page(s) 16–25

Abstract: Vibrio cholerae has become a model organism for studies connecting virulence, pathogen evolution and infectious disease ecology. The coordinate expression of motility, virulence and biofilm enhances its pathogenicity, environmental fitness and fecal-oral ...

Abstract	Vibrio cholerae has become a model organism for studies connecting virulence, pathogen evolution and infectious disease ecology. The coordinate expression of motility, virulence and biofilm enhances its pathogenicity, environmental fitness and fecal-oral transmission. The histone-like nucleoid structuring protein negatively regulates gene expression at multiple phases of the V. cholerae life cycle. Here we discuss: (i) the regulatory and structural implications of H-NS chromatin-binding in the two-chromosome cholera bacterium; (ii) the factors that counteract H-NS repression; and (iii) a model for the regulation of the V. cholerae life cycle that integrates H-NS repression, cyclic diguanylic acid signaling and the general stress response.
MeSH term(s)	Bacterial Proteins/metabolism ; Biofilms/growth & development ; Chromatin/metabolism ; DNA-Binding Proteins/metabolism ; Gene Expression Regulation, Bacterial ; Locomotion ; Protein Binding ; Vibrio cholerae/genetics ; Vibrio cholerae/physiology ; Virulence
Chemical Substances	Bacterial Proteins ; Chromatin ; DNA-Binding Proteins ; H-NS protein, bacteria
Language	English
Publishing date	2017-01
Publishing country	France
Document type	Journal Article ; Review
ZDB-ID	1004220-9
ISSN	1769-7123 ; 0923-2508
ISSN (online)	1769-7123
ISSN	0923-2508
DOI	10.1016/j.resmic.2016.07.007
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Zs.A 890: Show issues

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Article ; Online: 3-Amino 1,8-naphthalimide, a structural analog of the anti-cholera drug virstatin inhibits chemically-biased swimming and swarming motility in vibrios.

Wang, Hongxia / Silva, Anisia J / Benitez, Jorge A

Microbes and infection

2017 Volume 19, Issue 6, Page(s) 370–375

Abstract: A screen for inhibitors of Vibrio cholerae motility identified the compound 3-amino 1,8-naphthalimide (3-A18NI), a structural analog of the cholera drug virstatin. Similar to virstatin, 3-A18NI diminished cholera toxin production. In contrast, 3-A18NI ... ...

Abstract	A screen for inhibitors of Vibrio cholerae motility identified the compound 3-amino 1,8-naphthalimide (3-A18NI), a structural analog of the cholera drug virstatin. Similar to virstatin, 3-A18NI diminished cholera toxin production. In contrast, 3-A18NI impeded swimming and/or swarming motility of V. cholerae and V. parahemolyticus suggesting that it could target the chemotaxis pathway shared by the polar and lateral flagellar system of vibrios. 3-A18NI did not inhibit the expression of V. cholerae major flagellin FlaA or the assembly of its polar flagellum. Finally, 3-A18NI enhanced V. cholerae colonization mimicking the phenotype of chemotaxis mutants that exhibit counterclockwise-biased flagellum rotation.
Language	English
Publishing date	2017-06
Publishing country	France
Document type	Journal Article
ZDB-ID	1465093-9
ISSN	1769-714X ; 1286-4579
ISSN (online)	1769-714X
ISSN	1286-4579
DOI	10.1016/j.micinf.2017.03.003
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Zs.A 5014: Show issues

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Article: A proteome-wide screen to identify transcription factors interacting with the Vibrio cholerae rpoS promoter

Ayala, Julio C / Benitez, Jorge A / Silva, Anisia J

Journal of microbiological methods. 2019 Aug. 23,

2019

Abstract	We describe a proteomic approach to identify transcription factors binding to a target promoter. The method's usefulness was tested by identifying proteins binding to the Vibrio cholerae rpoS promoter in response to cell density. Proteins identified in this screen included the nucleoid-associated protein Fis and the quorum sensing regulator HapR.
Keywords	Vibrio cholerae ; proteomics ; quorum sensing ; transcription factors
Language	English
Dates of publication	2019-0823
Publishing place	Elsevier B.V.
Document type	Article
Note	Pre-press version
ZDB-ID	604916-3
ISSN	1872-8359 ; 0167-7012
ISSN (online)	1872-8359
ISSN	0167-7012
DOI	10.1016/j.mimet.2019.105702
Database	NAL-Catalogue (AGRICOLA)

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Zs.A 1849: Show issues

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Article ; Online: Deletion of gene encoding the nucleoid-associated protein H-NS unmasks hidden regulatory connections in El Tor biotype Vibrio cholerae.

Russell, Raedeen / Wang, Hongxia / Benitez, Jorge A / Silva, Anisia J

Microbiology (Reading, England)

2018 Volume 164, Issue 7, Page(s) 998–1003

Abstract: Hypervirulent atypical El Tor biotype Vibrio cholerae O1 isolates harbour mutations in the DNA-binding domain of the nucleoid-associated protein H-NS and the receiver domain of the response regulator VieA. Here, we provide two examples in which ... ...

Abstract	Hypervirulent atypical El Tor biotype Vibrio cholerae O1 isolates harbour mutations in the DNA-binding domain of the nucleoid-associated protein H-NS and the receiver domain of the response regulator VieA. Here, we provide two examples in which inactivation of H-NS in El Tor biotype vibrios unmasks hidden regulatory connections. First, deletion of the helix-turn-helix domain of VieA in an hns mutant background diminished biofilm formation and exopolysaccharide gene expression, a function that phenotypically opposes its phosphodiesterase activity. Second, deletion of vieA in an hns mutant diminished the expression of σ
MeSH term(s)	Bacterial Proteins/genetics ; Biofilms/growth & development ; DNA-Binding Proteins/genetics ; Gene Deletion ; Gene Expression Regulation, Bacterial ; Mutation ; Polysaccharides, Bacterial/genetics ; Sigma Factor/genetics ; Stress, Physiological/genetics ; Vibrio cholerae O1/genetics ; Vibrio cholerae O1/pathogenicity ; Vibrio cholerae O1/physiology ; Virulence/genetics
Chemical Substances	Bacterial Proteins ; DNA-Binding Proteins ; H-NS protein, bacteria ; Polysaccharides, Bacterial ; Sigma Factor ; VieA protein, Vibrio cholerae ; sporulation-specific sigma factors
Language	English
Publishing date	2018-05-29
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	1180712-x
ISSN	1465-2080 ; 1350-0872
ISSN (online)	1465-2080
ISSN	1350-0872
DOI	10.1099/mic.0.000672
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Article ; Online: Flagellar motility, extracellular proteases and Vibrio cholerae detachment from abiotic and biotic surfaces.

Mewborn, Loree / Benitez, Jorge A / Silva, Anisia J

Microbial pathogenesis

2017 Volume 113, Page(s) 17–24

Abstract: Vibrio cholerae of serogroups O1 and O139, the causative agent of Asiatic cholera, continues to be a major global health threat. This pathogen utilizes substratum-specific pili to attach to distinct surfaces in the aquatic environment and the human small ...

Abstract	Vibrio cholerae of serogroups O1 and O139, the causative agent of Asiatic cholera, continues to be a major global health threat. This pathogen utilizes substratum-specific pili to attach to distinct surfaces in the aquatic environment and the human small intestine and detaches when conditions become unfavorable. Both attachment and detachment are critical to bacterial environmental survival, pathogenesis and disease transmission. However, the factors that promote detachment are less understood. In this study, we examine the role of flagellar motility and hemagglutinin/protease (HapA) in vibrio detachment from a non-degradable abiotic surface and from the suckling mouse intestine. Flagellar motility facilitated V. cholerae detachment from abiotic surfaces. HapA had no effect on the stability of biofilms formed on abiotic surfaces despite representing >50% of the proteolytic activity present in the extracellular matrix. We developed a balanced lethal plasmid system to increase the bacterial cyclic diguanylate (c-di-GMP) pool late in infection, a condition that represses motility and HapA expression. Increasing the c-di-GMP pool enhanced V. cholerae colonization of the suckling mouse intestine. The c-di-GMP effect was fully abolished in hapA isogenic mutants. These results suggest that motility facilitates detachment in a substratum-independent manner. Instead, HapA appears to function as a substratum-specific detachment factor.
MeSH term(s)	Animals ; Bacterial Adhesion/physiology ; Biofilms/growth & development ; Cholera/microbiology ; Cyclic GMP/analogs & derivatives ; Cyclic GMP/metabolism ; Fimbriae, Bacterial/physiology ; Flagella/physiology ; Gene Expression Regulation, Bacterial ; Intestinal Mucosa/microbiology ; Intestine, Small/microbiology ; Metalloendopeptidases/genetics ; Metalloendopeptidases/metabolism ; Mice ; Movement/physiology ; Polystyrenes ; Vibrio cholerae/genetics ; Vibrio cholerae/metabolism
Chemical Substances	Polystyrenes ; bis(3',5')-cyclic diguanylic acid (61093-23-0) ; Metalloendopeptidases (EC 3.4.24.-) ; hemagglutinin-protease (EC 3.4.24.-) ; Cyclic GMP (H2D2X058MU)
Language	English
Publishing date	2017-12
Publishing country	England
Document type	Journal Article
ZDB-ID	632772-2
ISSN	1096-1208 ; 0882-4010
ISSN (online)	1096-1208
ISSN	0882-4010
DOI	10.1016/j.micpath.2017.10.016
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Zs.A 2136: Show issues

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Article ; Online: Vibrio cholerae Biofilms and Cholera Pathogenesis.

Anisia J Silva / Jorge A Benitez

PLoS Neglected Tropical Diseases, Vol 10, Iss 2, p e

2016 Volume 0004330

Abstract	Vibrio cholerae can switch between motile and biofilm lifestyles. The last decades have been marked by a remarkable increase in our knowledge of the structure, regulation, and function of biofilms formed under laboratory conditions. Evidence has grown suggesting that V. cholerae can form biofilm-like aggregates during infection that could play a critical role in pathogenesis and disease transmission. However, the structure and regulation of biofilms formed during infection, as well as their role in intestinal colonization and virulence, remains poorly understood. Here, we review (i) the evidence for biofilm formation during infection, (ii) the coordinate regulation of biofilm and virulence gene expression, and (iii) the host signals that favor V. cholerae transitions between alternative lifestyles during intestinal colonization, and (iv) we discuss a model for the role of V. cholerae biofilms in pathogenicity.
Keywords	Arctic medicine. Tropical medicine ; RC955-962 ; Public aspects of medicine ; RA1-1270
Language	English
Publishing date	2016-02-01T00:00:00Z
Publisher	Public Library of Science (PLoS)
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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