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Article ; Online: Lymphostatin, a virulence factor of attaching and effacing

Ruamsap, Nattaya / Riyapa, Donporn / Janesomboon, Sujintana / Stevens, Joanne M / Pichyangkul, Sathit / Pattanapanyasat, Kovit / Demons, Samandra T / Stevens, Mark P / Korbsrisate, Sunee

Frontiers in cellular and infection microbiology

2022 Volume 12, Page(s) 941939

Abstract: Lymphostatin is a virulence factor of ... ...

Abstract	Lymphostatin is a virulence factor of enteropathogenic
MeSH term(s)	Apoptosis ; Bacterial Toxins/immunology ; CD8-Positive T-Lymphocytes/immunology ; Cell Cycle Checkpoints/immunology ; Cell Division ; Cell Proliferation/physiology ; Cytokines/biosynthesis ; Cytokines/immunology ; Enteropathogenic Escherichia coli/immunology ; Enteropathogenic Escherichia coli/pathogenicity ; Escherichia coli/immunology ; Escherichia coli/pathogenicity ; Escherichia coli Infections/immunology ; Escherichia coli Proteins/immunology ; Humans ; Interleukin-2 ; Interleukin-4 ; Leukocytes, Mononuclear/immunology ; Necrosis ; T-Lymphocytes/immunology ; Virulence Factors/immunology
Chemical Substances	Bacterial Toxins ; Cytokines ; Escherichia coli Proteins ; Interleukin-2 ; Virulence Factors ; lymphostatin protein, E coli ; Interleukin-4 (207137-56-2)
Language	English
Publishing date	2022-07-29
Publishing country	Switzerland
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2619676-1
ISSN	2235-2988 ; 2235-2988
ISSN (online)	2235-2988
ISSN	2235-2988
DOI	10.3389/fcimb.2022.941939
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Article ; Online: Transketolase and vitamin B1 influence on ROS-dependent neutrophil extracellular traps (NETs) formation.

Riyapa, Donporn / Rinchai, Darawan / Muangsombut, Veerachat / Wuttinontananchai, Chayanin / Toufiq, Mohammed / Chaussabel, Damien / Ato, Manabu / Blackwell, Jenefer M / Korbsrisate, Sunee

PloS one

2019 Volume 14, Issue 8, Page(s) e0221016

Abstract: Neutrophil extracellular traps (NETs) are a recently identified, web-like, extracellular structure composed of decondensed nuclear DNA and associated antimicrobial granules. NETs are extruded into the extracellular environment via the reactive oxygen ... ...

Abstract	Neutrophil extracellular traps (NETs) are a recently identified, web-like, extracellular structure composed of decondensed nuclear DNA and associated antimicrobial granules. NETs are extruded into the extracellular environment via the reactive oxygen species (ROS)-dependent cell death pathway participating in inflammation and autoimmune diseases. Transketolase (TKT) is a thiamine pyrophosphate (vitamin B1)-dependent enzyme that links the pentose phosphate pathway with the glycolytic pathway by feeding excess sugar phosphates into the main carbohydrate metabolic pathways to generate biosynthetic reducing capacity in the form of NADPH as a substrate for ROS generation. In this work, TKT was selected as a lead candidate from 24 NET-associated proteins obtained by literature screening and knowledge gap assessment. Consequently, we determined whether TKT influenced NET formation in vitro. We firstly established that the release of ROS-dependent NETs was significantly decreased after purified human PMNs were pretreated with oxythiamine, a TKT inhibitor, and in a concentration dependent manner. As a cofactor for TKT reaction, we evaluated the release of NET formation either in vitamin B1 treatment or in combined use of oxythiamine and vitamin B1, and found that those treatments also exerted a significant suppressive effect on the amount of NET-DNA and ROS production. The regulation of TKT by oxythiamine and/or vitamin B1 may therefore be associated with response to the modulation of NET formation by preventing generation of excessive NETs in inflammatory diseases.
MeSH term(s)	Extracellular Traps/metabolism ; Humans ; Inflammation/metabolism ; Inflammation/pathology ; Neutrophils/metabolism ; Neutrophils/pathology ; Reactive Oxygen Species/metabolism ; Thiamine/metabolism ; Transketolase/metabolism
Chemical Substances	Reactive Oxygen Species ; Transketolase (EC 2.2.1.1) ; Thiamine (X66NSO3N35)
Language	English
Publishing date	2019-08-15
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	1932-6203
ISSN (online)	1932-6203
DOI	10.1371/journal.pone.0221016
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Article: Burkholderia pseudomallei-induced cell fusion in U937 macrophages can be inhibited by monoclonal antibodies against host cell surface molecules

Suparak, Supaporn / Muangsombut, Veerachat / Riyapa, Donporn / Stevens, Joanne M / Stevens, Mark P / Lertmemongkolchai, Ganjana / Korbsrisate, Sunee

Microbes and Infection. 2011 Nov., v. 13, no. 12-13

2011

Abstract: Burkholderia pseudomallei induces the formation of multinucleated giant cells in cell monolayers. After infection of human macrophage-like U937 cells with B. pseudomallei, addition of monoclonal antibodies against integrin-associated protein (CD47), E- ... ...

Abstract	Burkholderia pseudomallei induces the formation of multinucleated giant cells in cell monolayers. After infection of human macrophage-like U937 cells with B. pseudomallei, addition of monoclonal antibodies against integrin-associated protein (CD47), E-selectin (CD62E), a fusion regulatory protein (CD98), and E-cadherin (CD324) suppressed multinucleated giant cells in a concentration-dependent manner while monoclonal antibodies against other surface molecules did not inhibit fusion despite binding to the cell surface. Flow cytometric analysis showed increased expression of CD47 and CD98, but not CD62E and CD324, upon B. pseudomallei infection. Our data suggest the involvement of specific cellular factors in the process of B. pseudomallei-induced fusion.
Keywords	Burkholderia pseudomallei ; cell fusion ; flow cytometry ; giant cells ; human diseases ; macrophages ; monoclonal antibodies ; regulatory proteins
Language	English
Dates of publication	2011-11
Size	p. 1006-1011.
Publishing place	Elsevier Masson SAS
Document type	Article
ZDB-ID	1465093-9
ISSN	1769-714X ; 1286-4579
ISSN (online)	1769-714X
ISSN	1286-4579
DOI	10.1016/j.micinf.2011.06.007
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Article ; Online: Neutrophil extracellular traps exhibit antibacterial activity against burkholderia pseudomallei and are influenced by bacterial and host factors.

Riyapa, Donporn / Buddhisa, Surachat / Korbsrisate, Sunee / Cuccui, Jon / Wren, Brendan W / Stevens, Mark P / Ato, Manabu / Lertmemongkolchai, Ganjana

Infection and immunity

2012 Volume 80, Issue 11, Page(s) 3921–3929

Abstract: Burkholderia pseudomallei is the causative pathogen of melioidosis, of which a major predisposing factor is diabetes mellitus. Polymorphonuclear neutrophils (PMNs) kill microbes extracellularly by the release of neutrophil extracellular traps (NETs). ... ...

Abstract	Burkholderia pseudomallei is the causative pathogen of melioidosis, of which a major predisposing factor is diabetes mellitus. Polymorphonuclear neutrophils (PMNs) kill microbes extracellularly by the release of neutrophil extracellular traps (NETs). PMNs play a key role in the control of melioidosis, but the involvement of NETs in killing of B. pseudomallei remains obscure. Here, we showed that bactericidal NETs were released from human PMNs in response to B. pseudomallei in a dose- and time-dependent manner. B. pseudomallei-induced NET formation required NADPH oxidase activation but not phosphatidylinositol-3 kinase, mitogen-activated protein kinases, or Src family kinase signaling pathways. B. pseudomallei mutants defective in the virulence-associated Bsa type III protein secretion system (T3SS) or capsular polysaccharide I (CPS-I) induced elevated levels of NETs. NET induction by such mutants was associated with increased bacterial killing, phagocytosis, and oxidative burst by PMNs. Taken together the data imply that T3SS and the capsule may play a role in evading the induction of NETs. Importantly, PMNs from diabetic subjects released NETs at a lower level than PMNs from healthy subjects. Modulation of NET formation may therefore be associated with the pathogenesis and control of melioidosis.
MeSH term(s)	Antibodies, Bacterial/analysis ; Bacterial Proteins ; Burkholderia pseudomallei/immunology ; Burkholderia pseudomallei/pathogenicity ; Cells, Cultured ; Fluorescent Antibody Technique ; Humans ; Melioidosis/immunology ; Microbial Viability ; Neutrophils/immunology ; Phagocytosis ; Respiratory Burst/immunology ; Virulence ; Virulence Factors
Chemical Substances	Antibodies, Bacterial ; Bacterial Proteins ; Virulence Factors
Language	English
Publishing date	2012-08-27
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	218698-6
ISSN	1098-5522 ; 0019-9567
ISSN (online)	1098-5522
ISSN	0019-9567
DOI	10.1128/IAI.00806-12
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Article ; Online: Macroautophagy is essential for killing of intracellular Burkholderia pseudomallei in human neutrophils.

Rinchai, Darawan / Riyapa, Donporn / Buddhisa, Surachat / Utispan, Kusumawadee / Titball, Richard W / Stevens, Mark P / Stevens, Joanne M / Ogawa, Michinaga / Tanida, Isei / Koike, Masato / Uchiyama, Yasuo / Ato, Manabu / Lertmemongkolchai, Ganjana

Autophagy

2015 Volume 11, Issue 5, Page(s) 748–755

Abstract: Neutrophils play a key role in the control of Burkholderia pseudomallei, the pathogen that causes melioidosis. Here, we show that survival of intracellular B. pseudomallei was significantly increased in the presence of 3-methyladenine or lysosomal ... ...

Abstract	Neutrophils play a key role in the control of Burkholderia pseudomallei, the pathogen that causes melioidosis. Here, we show that survival of intracellular B. pseudomallei was significantly increased in the presence of 3-methyladenine or lysosomal cathepsin inhibitors. The LC3-flux was increased in B. pseudomallei-infected neutrophils. Concordant with this result, confocal microscopy analyses using anti-LC3 antibodies revealed that B. pseudomallei-containing phagosomes partially overlapped with LC3-positive signal at 3 and 6 h postinfection. Electron microscopic analyses of B. pseudomallei-infected neutrophils at 3 h revealed B. pseudomallei-containing phagosomes that occasionally fused with phagophores or autophagosomes. Following infection with a B. pseudomallei mutant lacking the Burkholderia secretion apparatus Bsa Type III secretion system, neither this characteristic structure nor bacterial escape into the cytosol were observed. These findings indicate that human neutrophils are able to recruit autophagic machinery adjacent to B. pseudomallei-containing phagosomes in a Type III secretion system-dependent manner.
MeSH term(s)	Autophagy ; Bacterial Secretion Systems ; Biomarkers/metabolism ; Burkholderia pseudomallei/physiology ; Burkholderia pseudomallei/ultrastructure ; Cytoplasmic Granules/metabolism ; Cytosol/metabolism ; Humans ; Intracellular Space/microbiology ; Lysosomal Membrane Proteins/metabolism ; Lysosomes/metabolism ; Lysosomes/ultrastructure ; Microbial Viability ; Microtubule-Associated Proteins/metabolism ; Neutrophils/microbiology ; Neutrophils/ultrastructure ; Phagosomes/metabolism ; Phagosomes/ultrastructure
Chemical Substances	Bacterial Secretion Systems ; Biomarkers ; LAMP1 protein, human ; Lysosomal Membrane Proteins ; MAP1LC3A protein, human ; Microtubule-Associated Proteins
Language	English
Publishing date	2015-06-03
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2454135-7
ISSN	1554-8635 ; 1554-8627
ISSN (online)	1554-8635
ISSN	1554-8627
DOI	10.1080/15548627.2015.1040969
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Article ; Online: Burkholderia pseudomallei-induced cell fusion in U937 macrophages can be inhibited by monoclonal antibodies against host cell surface molecules.

Suparak, Supaporn / Muangsombut, Veerachat / Riyapa, Donporn / Stevens, Joanne M / Stevens, Mark P / Lertmemongkolchai, Ganjana / Korbsrisate, Sunee

Microbes and infection

2011 Volume 13, Issue 12-13, Page(s) 1006–1011

Abstract	Burkholderia pseudomallei induces the formation of multinucleated giant cells in cell monolayers. After infection of human macrophage-like U937 cells with B. pseudomallei, addition of monoclonal antibodies against integrin-associated protein (CD47), E-selectin (CD62E), a fusion regulatory protein (CD98), and E-cadherin (CD324) suppressed multinucleated giant cells in a concentration-dependent manner while monoclonal antibodies against other surface molecules did not inhibit fusion despite binding to the cell surface. Flow cytometric analysis showed increased expression of CD47 and CD98, but not CD62E and CD324, upon B. pseudomallei infection. Our data suggest the involvement of specific cellular factors in the process of B. pseudomallei-induced fusion.
MeSH term(s)	Animals ; Antibodies, Bacterial/immunology ; Antibodies, Monoclonal/immunology ; Burkholderia pseudomallei/immunology ; Burkholderia pseudomallei/physiology ; CD47 Antigen/immunology ; CD47 Antigen/metabolism ; Cadherins/immunology ; Cadherins/metabolism ; Cell Fusion ; E-Selectin/immunology ; E-Selectin/metabolism ; Fusion Regulatory Protein-1/immunology ; Fusion Regulatory Protein-1/metabolism ; Giant Cells/physiology ; Humans ; Macrophages/immunology ; Macrophages/microbiology ; Mice ; Rats ; U937 Cells
Chemical Substances	Antibodies, Bacterial ; Antibodies, Monoclonal ; CD47 Antigen ; CD47 protein, human ; Cadherins ; E-Selectin ; Fusion Regulatory Protein-1
Language	English
Publishing date	2011-07-06
Publishing country	France
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1465093-9
ISSN	1769-714X ; 1286-4579
ISSN (online)	1769-714X
ISSN	1286-4579
DOI	10.1016/j.micinf.2011.06.007
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Article: Burkholderia pseudomallei Proteins Presented by Monocyte-Derived Dendritic Cells Stimulate Human Memory T Cells In Vitro

Tippayawat, Patcharaporn / Pinsiri, Maneerat / Rinchai, Darawan / Riyapa, Donporn / Romphruk, Amornrat / Gan, Yunn-Hwen / Houghton, Raymond L / Felgner, Philip L / Titball, Richard W / Stevens, Mark P / Galyov, Edouard E / Bancroft, Gregory J / Lertmemongkolchai, Ganjana

Infection and immunity. 2011 Jan., v. 79, no. 1

2011

Abstract: Melioidosis is a severe infectious disease caused by the saprophytic facultative intracellular pathogen Burkholderia pseudomallei. The disease is endemic in Southeast Asia and Northern Australia, and no effective vaccine exists. To describe human cell- ... ...

Abstract	Melioidosis is a severe infectious disease caused by the saprophytic facultative intracellular pathogen Burkholderia pseudomallei. The disease is endemic in Southeast Asia and Northern Australia, and no effective vaccine exists. To describe human cell-mediated immune responses to B. pseudomallei and to identify candidate antigens for vaccine development, the ability of antigen-pulsed monocyte-derived dendritic cells (moDCs) to trigger autologous T-cell responses to B. pseudomallei and its products was tested. moDCs were prepared from healthy individuals exposed or not exposed to B. pseudomallei, based on serological evidence. These were pulsed with heat-killed B. pseudomallei or purified antigens, including ABC transporters (LolC, OppA, and PotF), Bsa type III secreted proteins (BipD and BopE), tandem repeat sequence-containing proteins (Rp1 and Rp2), flagellin, and heat shock proteins (Hsp60 and Hsp70), prior to being mixed with autologous T-cell populations. After pulsing of cells with either heat-killed B. pseudomallei, LolC, or Rp2, coculturing the antigen-pulsed moDCs with T cells elicited gamma interferon production from CD4⁺ T cells from seropositive donors at levels greater than those for seronegative donors. These antigens also induced granzyme B (cytotoxic) responses from CD8⁺ T cells. Activation of antigen-specific CD4⁺ T cells required direct contact with moDCs and was therefore not dependent on soluble mediators. Rp peptide epitopes recognized by T cells in healthy individuals were identified. Our study provides valuable novel data on the induction of human cell-mediated immune responses to B. pseudomallei and its protein antigens that may be exploited in the rational development of vaccines to combat melioidosis.
Keywords	ABC transporters ; Burkholderia pseudomallei ; CD4-positive T-lymphocytes ; CD8-positive T-lymphocytes ; cell-mediated immunity ; cytotoxicity ; dendritic cells ; direct contact ; epitopes ; flagellin ; heat shock proteins ; humans ; interferon-gamma ; melioidosis ; pathogens ; saprophytes ; seroprevalence ; vaccine development ; Australia ; South East Asia
Language	English
Size	p. 305-313.
Publishing place	American Society for Microbiology
Document type	Article
ZDB-ID	218698-6
ISSN	1098-5522 ; 0019-9567
ISSN (online)	1098-5522
ISSN	0019-9567
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Article ; Online: Burkholderia pseudomallei proteins presented by monocyte-derived dendritic cells stimulate human memory T cells in vitro.

Infection and immunity

2010 Volume 79, Issue 1, Page(s) 305–313

Abstract	Melioidosis is a severe infectious disease caused by the saprophytic facultative intracellular pathogen Burkholderia pseudomallei. The disease is endemic in Southeast Asia and Northern Australia, and no effective vaccine exists. To describe human cell-mediated immune responses to B. pseudomallei and to identify candidate antigens for vaccine development, the ability of antigen-pulsed monocyte-derived dendritic cells (moDCs) to trigger autologous T-cell responses to B. pseudomallei and its products was tested. moDCs were prepared from healthy individuals exposed or not exposed to B. pseudomallei, based on serological evidence. These were pulsed with heat-killed B. pseudomallei or purified antigens, including ABC transporters (LolC, OppA, and PotF), Bsa type III secreted proteins (BipD and BopE), tandem repeat sequence-containing proteins (Rp1 and Rp2), flagellin, and heat shock proteins (Hsp60 and Hsp70), prior to being mixed with autologous T-cell populations. After pulsing of cells with either heat-killed B. pseudomallei, LolC, or Rp2, coculturing the antigen-pulsed moDCs with T cells elicited gamma interferon production from CD4(+) T cells from seropositive donors at levels greater than those for seronegative donors. These antigens also induced granzyme B (cytotoxic) responses from CD8(+) T cells. Activation of antigen-specific CD4(+) T cells required direct contact with moDCs and was therefore not dependent on soluble mediators. Rp peptide epitopes recognized by T cells in healthy individuals were identified. Our study provides valuable novel data on the induction of human cell-mediated immune responses to B. pseudomallei and its protein antigens that may be exploited in the rational development of vaccines to combat melioidosis.
MeSH term(s)	Bacterial Proteins/metabolism ; Burkholderia pseudomallei/immunology ; Burkholderia pseudomallei/metabolism ; CD4-Positive T-Lymphocytes/physiology ; Dendritic Cells/metabolism ; Endemic Diseases ; Epitopes, T-Lymphocyte ; Gene Expression Regulation, Bacterial ; Hot Temperature ; Humans ; Melioidosis/epidemiology ; Melioidosis/immunology ; Melioidosis/microbiology ; Serine Proteases ; Tandem Repeat Sequences
Chemical Substances	Bacterial Proteins ; Epitopes, T-Lymphocyte ; Serine Proteases (EC 3.4.-)
Language	English
Publishing date	2010-11-01
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	218698-6
ISSN	1098-5522 ; 0019-9567
ISSN (online)	1098-5522
ISSN	0019-9567
DOI	10.1128/IAI.00803-10
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