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Article ; Online: In Search of Spectroscopic Signatures of Periodontitis: A SERS-Based Magnetomicrofluidic Sensor for Detection of

Witkowska, Evelin / Łasica, Anna M / Niciński, Krzysztof / Potempa, Jan / Kamińska, Agnieszka

ACS sensors

2021 Volume 6, Issue 4, Page(s) 1621–1635

Abstract: Recently, ...

Abstract	Recently,
MeSH term(s)	Aggregatibacter actinomycetemcomitans ; Humans ; Periodontitis/diagnosis ; Porphyromonas gingivalis
Language	English
Publishing date	2021-04-01
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	2379-3694
ISSN (online)	2379-3694
DOI	10.1021/acssensors.1c00166
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Article: An Experimental Study of Possible Post-War Ferronickel Slag Waste Disposal in Szklary (Lower Silesian, Poland) as Partial Aggregate Substitute in Concrete: Characterization of Physical, Mechanical, and Thermal Properties.

Małek, Marcin / Jackowski, Mateusz / Łasica, Waldemar / Dydek, Kamil / Boczkowska, Anna

Materials (Basel, Switzerland)

2021 Volume 14, Issue 10

Abstract: Aggregates derived from waste, due to the growing awareness of global warming, are more and more often used in the concrete production process. This way, their disposal not only reduces the pollution of the Earth but also lowers the consumption of ... ...

Abstract	Aggregates derived from waste, due to the growing awareness of global warming, are more and more often used in the concrete production process. This way, their disposal not only reduces the pollution of the Earth but also lowers the consumption of natural aggregates, which are limited. One of the new "eco" aggregates may be a ferronickel slag waste (FNSW), which was generated in post-war metallurgical processes and stored in Szklary (Lower Silesian, Poland). In order to determine the possibility of using ferronickel slag waste aggregate (FNSWA) in the concrete production process, new concrete mixtures were designed and tested. Physical properties (cone slump, air content, pH, and density), mechanical properties (compressive strength, flexural strength, and tensile strength), and thermal properties (thermal conductivity) were assessed for all new laboratory recipes. Moreover, the modulus of elasticity and Poisson's ratio were determined. This study includes five different contents of FNSWA in the amount of 5%, 10%, 15%, 20%, and 25% of the mass of natural aggregate as its partial substitute. The final results were compared to the base sample (BS) containing 100% natural aggregate, which was granite.
Language	English
Publishing date	2021-05-14
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2487261-1
ISSN	1996-1944
ISSN	1996-1944
DOI	10.3390/ma14102552
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Article ; Online: The Type IX Secretion System (T9SS): Highlights and Recent Insights into Its Structure and Function.

Lasica, Anna M / Ksiazek, Miroslaw / Madej, Mariusz / Potempa, Jan

Frontiers in cellular and infection microbiology

2017 Volume 7, Page(s) 215

Abstract: Protein secretion systems are vital for prokaryotic life, as they enable bacteria to acquire nutrients, communicate with other species, defend against biological and chemical agents, and facilitate disease through the delivery of virulence factors. In ... ...

Abstract	Protein secretion systems are vital for prokaryotic life, as they enable bacteria to acquire nutrients, communicate with other species, defend against biological and chemical agents, and facilitate disease through the delivery of virulence factors. In this review, we will focus on the recently discovered type IX secretion system (T9SS), a complex translocon found only in some species of the
MeSH term(s)	Bacterial Proteins/metabolism ; Bacterial Secretion Systems/chemistry ; Bacterial Secretion Systems/physiology ; Bacteroidetes/physiology ; Flavobacterium/physiology ; Humans ; Porphyromonas gingivalis/pathogenicity ; Porphyromonas gingivalis/physiology ; Protein Processing, Post-Translational ; Protein Transport ; Virulence Factors
Chemical Substances	Bacterial Proteins ; Bacterial Secretion Systems ; Virulence Factors
Language	English
Publishing date	2017-05-26
Publishing country	Switzerland
Document type	Journal Article ; Review
ZDB-ID	2619676-1
ISSN	2235-2988 ; 2235-2988
ISSN (online)	2235-2988
ISSN	2235-2988
DOI	10.3389/fcimb.2017.00215
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Article ; Online: PorZ, an Essential Component of the Type IX Secretion System of

Madej, Mariusz / Nowakowska, Zuzanna / Ksiazek, Miroslaw / Lasica, Anna M / Mizgalska, Danuta / Nowak, Magdalena / Jacula, Anna / Bzowska, Monika / Scavenius, Carsten / Enghild, Jan J / Aduse-Opoku, Joseph / Curtis, Michael A / Gomis-Rüth, F Xavier / Potempa, Jan

mBio

2021 Volume 12, Issue 1

Abstract: Cargo proteins of the type IX secretion system (T9SS) in human pathogens from the Bacteroidetes phylum invariably possess a conserved C-terminal domain (CTD) that functions as a signal for outer membrane (OM) translocation. ... ...

Abstract	Cargo proteins of the type IX secretion system (T9SS) in human pathogens from the Bacteroidetes phylum invariably possess a conserved C-terminal domain (CTD) that functions as a signal for outer membrane (OM) translocation. In
MeSH term(s)	Aminoacyltransferases/metabolism ; Bacterial Proteins/genetics ; Bacterial Proteins/metabolism ; Bacterial Secretion Systems/genetics ; Bacterial Secretion Systems/metabolism ; Cysteine Endopeptidases/metabolism ; Lipopolysaccharides/metabolism ; Peptidyl Transferases/genetics ; Peptidyl Transferases/metabolism ; Porphyromonas gingivalis/enzymology ; Porphyromonas gingivalis/genetics ; Porphyromonas gingivalis/metabolism ; Protein Binding ; Protein Processing, Post-Translational ; Protein Transport
Chemical Substances	Bacterial Proteins ; Bacterial Secretion Systems ; Lipopolysaccharides ; Aminoacyltransferases (EC 2.3.2.-) ; sortase A (EC 2.3.2.-) ; Peptidyl Transferases (EC 2.3.2.12) ; Cysteine Endopeptidases (EC 3.4.22.-)
Language	English
Publishing date	2021-02-23
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2557172-2
ISSN	2150-7511 ; 2161-2129
ISSN (online)	2150-7511
ISSN	2161-2129
DOI	10.1128/mBio.02262-20
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Article ; Online: Enhancement of direct electron transfer in graphene bioelectrodes containing novel cytochrome c

Izzo, Miriam / Osella, Silvio / Jacquet, Margot / Kiliszek, Małgorzata / Harputlu, Ersan / Starkowska, Alicja / Łasica, Anna / Unlu, C Gokhan / Uśpieński, Tomasz / Niewiadomski, Paweł / Bartosik, Dariusz / Trzaskowski, Bartosz / Ocakoglu, Kasim / Kargul, Joanna

Bioelectrochemistry (Amsterdam, Netherlands)

2021 Volume 140, Page(s) 107818

Abstract: The highly efficient bioelectrodes based on single layer graphene (SLG) functionalized with pyrene self-assembled monolayer and novel ... ...

Abstract	The highly efficient bioelectrodes based on single layer graphene (SLG) functionalized with pyrene self-assembled monolayer and novel cytochromec
MeSH term(s)	Amino Acid Sequence ; Cytochrome c Group/chemistry ; Cytochrome c Group/genetics ; Electrodes ; Electron Transport ; Graphite/chemistry ; Heme ; Mutation
Chemical Substances	Cytochrome c Group ; cytochrome c553 ; Heme (42VZT0U6YR) ; Graphite (7782-42-5)
Language	English
Publishing date	2021-04-08
Publishing country	Netherlands
Document type	Journal Article
ZDB-ID	2010650-6
ISSN	1878-562X ; 0302-4598 ; 1567-5394
ISSN (online)	1878-562X
ISSN	0302-4598 ; 1567-5394
DOI	10.1016/j.bioelechem.2021.107818
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Article ; Online: Bipolar disorder in the postpartum period: the impact of a prenatal mood episode on maternal improvement at postpartum discharge after joint inpatient hospitalization.

Lasica, Pierre-Alexandre / Glangeaud-Freudenthal, Nine M C / Falissard, Bruno / Sutter-Dallay, Anne-Laure / Gressier, Florence

Archives of women's mental health

2021 Volume 25, Issue 2, Page(s) 399–409

Abstract: Bipolar disorder (BD) is linked to a high risk of relapse in the year postpartum. The aim of this study was to search for an association of a mood episode during pregnancy with a lack of maternal improvement after a post-partum episode requiring joint ... ...

Abstract	Bipolar disorder (BD) is linked to a high risk of relapse in the year postpartum. The aim of this study was to search for an association of a mood episode during pregnancy with a lack of maternal improvement after a post-partum episode requiring joint hospitalization. In an observational, naturalist, and multicentric study, 261 women suffering from a BD and jointly hospitalized with their child in a Mother-Baby Unit (MBU) were assessed for risk factors associated with a lack of maternal improvement at discharge. A directed acyclic graph (DAG)-based approach was used to identify confounders to be included in a multiple regression model. In bivariate analyses, a lack of improvement (16.9%) was associated with pregnancy specificities (decompensation, psychotropic treatment, antipsychotics, and benzodiazepines intake), as well as maternal smoking during pregnancy and baby's neonatal hospitalization. In a multivariate analysis based on DAG, a lack of improvement was linked to psychiatric decompensation during pregnancy (OR = 3.31, 95%CI [1.55-7.35], p = 0.002), independently from maternal age, mother's maltreatment during childhood, low level of education, single status, low familial social support, and diagnosis of personality disorder. This study shows the critical importance of mental health during pregnancy in women with BD. Clinical screening and evaluation of the benefit/risk balance of psychotropics during pregnancy are essential.
MeSH term(s)	Bipolar Disorder/psychology ; Female ; Hospitalization ; Humans ; Infant, Newborn ; Inpatients ; Mothers/psychology ; Patient Discharge ; Postpartum Period/psychology ; Pregnancy
Language	English
Publishing date	2021-10-18
Publishing country	Austria
Document type	Journal Article
ZDB-ID	1463529-X
ISSN	1435-1102 ; 1434-1816
ISSN (online)	1435-1102
ISSN	1434-1816
DOI	10.1007/s00737-021-01188-3
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Article ; Online: Structural determinants of inhibition of Porphyromonas gingivalis gingipain K by KYT-36, a potent, selective, and bioavailable peptidase inhibitor.

Guevara, Tibisay / Rodríguez-Banqueri, Arturo / Lasica, Anna M / Ksiazek, Miroslaw / Potempa, Barbara A / Potempa, Jan / Gomis-Rüth, F Xavier

Scientific reports

2019 Volume 9, Issue 1, Page(s) 4935

Abstract: Porphyromonas gingivalis is a member of the dysbiotic oral microbiome and a "keystone pathogen" that causes severe periodontal disease, which is among the most prevalent infectious diseases. Part of the virulence factors secreted by P. gingivalis are the ...

Abstract	Porphyromonas gingivalis is a member of the dysbiotic oral microbiome and a "keystone pathogen" that causes severe periodontal disease, which is among the most prevalent infectious diseases. Part of the virulence factors secreted by P. gingivalis are the essential cysteine peptidases gingipain K (Kgp) and R (RgpA and RgpB), which account for 85% of the extracellular proteolytic activity of the pathogen and are thus prime targets for inhibition. We report the high-resolution (1.20 Å) complex structure of Kgp with KYT-36, a peptide-derived, potent, bioavailable and highly selective inhibitor, which is widely used for studies in vitro, in cells and in vivo. Sub-nanomolar inhibition of Kgp is achieved by tight binding to the active-site cleft, which is covered for its sub-sites S
MeSH term(s)	Bacteroidaceae Infections/drug therapy ; Bacteroidaceae Infections/microbiology ; Benzylamines/chemistry ; Benzylamines/pharmacology ; Benzylamines/therapeutic use ; Carbamates/chemistry ; Carbamates/pharmacology ; Carbamates/therapeutic use ; Catalytic Domain/drug effects ; Crystallography, X-Ray ; Drug Development ; Gingipain Cysteine Endopeptidases/antagonists & inhibitors ; Gingipain Cysteine Endopeptidases/metabolism ; Gingipain Cysteine Endopeptidases/ultrastructure ; Hydrazines/chemistry ; Hydrazines/pharmacology ; Hydrazines/therapeutic use ; Hydrophobic and Hydrophilic Interactions ; Periodontitis/drug therapy ; Periodontitis/microbiology ; Porphyromonas gingivalis/metabolism ; Porphyromonas gingivalis/pathogenicity ; Porphyromonas gingivalis/ultrastructure ; Protease Inhibitors/chemistry ; Protease Inhibitors/pharmacology ; Protease Inhibitors/therapeutic use ; Protein Domains ; Structure-Activity Relationship ; Virulence Factors/antagonists & inhibitors ; Virulence Factors/metabolism
Chemical Substances	Benzylamines ; Carbamates ; Gingipain Cysteine Endopeptidases ; Hydrazines ; KYT-36 ; Protease Inhibitors ; Virulence Factors
Language	English
Publishing date	2019-03-20
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2615211-3
ISSN	2045-2322 ; 2045-2322
ISSN (online)	2045-2322
ISSN	2045-2322
DOI	10.1038/s41598-019-41354-3
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Article: Engineering of Helicobacter pylori Dimeric Oxidoreductase DsbK (HP0231).

Bocian-Ostrzycka, Katarzyna M / Grzeszczuk, Magdalena J / Banaś, Anna M / Jastrząb, Katarzyna / Pisarczyk, Karolina / Kolarzyk, Anna / Łasica, Anna M / Collet, Jean-François / Jagusztyn-Krynicka, Elżbieta K

Frontiers in microbiology

2016 Volume 7, Page(s) 1158

Abstract: The formation of disulfide bonds that are catalyzed by proteins of the Dsb (disulfide bond) family is crucial for the correct folding of many extracytoplasmic proteins. Thus, this formation plays an essential, pivotal role in the assembly of many ... ...

Abstract	The formation of disulfide bonds that are catalyzed by proteins of the Dsb (disulfide bond) family is crucial for the correct folding of many extracytoplasmic proteins. Thus, this formation plays an essential, pivotal role in the assembly of many virulence factors. The Helicobacter pylori disulfide bond-forming system is uncomplicated compared to the best-characterized Escherichia coli Dsb pathways. It possesses only two extracytoplasmic Dsb proteins named HP0377 and HP0231. As previously shown, HP0377 is a reductase involved in the process of cytochrome c maturation. Additionally, it also possesses disulfide isomerase activity. HP0231 was the first periplasmic dimeric oxidoreductase involved in disulfide generation to be described. Although HP0231 function is critical for oxidative protein folding, its structure resembles that of dimeric EcDsbG, which does not confer this activity. However, the HP0231 catalytic motifs (CXXC and the so-called cis-Pro loop) are identical to that of monomeric EcDsbA. To understand the functioning of HP0231, we decided to study the relations between its sequence, structure and activity through an extensive analysis of various HP0231 point mutants, using in vivo and in vitro strategies. Our work shows the crucial role of the cis-Pro loop, as changing valine to threonine in this motif completely abolishes the protein function in vivo. Functioning of HP0231 is conditioned by the combination of CXXC and the cis-Pro loop, as replacing the HP0231 CXXC motif by the motif from EcDsbG or EcDsbC results in bifunctional protein, at least in E. coli. We also showed that the dimerization domain of HP0231 ensures contact with its substrates. Moreover, the activity of this oxidase is independent on the structure of the catalytic domain. Finally, we showed that HP0231 chaperone activity is independent of its redox function.
Language	English
Publishing date	2016-07-26
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2587354-4
ISSN	1664-302X
ISSN	1664-302X
DOI	10.3389/fmicb.2016.01158
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Article: The role of Dsb proteins of Gram-negative bacteria in the process of pathogenesis.

Łasica, Anna M / Jagusztyn-Krynicka, Elzbieta K

FEMS microbiology reviews

2007 Volume 31, Issue 5, Page(s) 626–636

Abstract: Tertiary and quaternary structures of extracytoplasmic proteins containing more than one cysteine residue often require introduction of disulfide bonds. This process takes place in an oxidative environment, such as the periplasm of Gram-negative bacteria, ...

Abstract	Tertiary and quaternary structures of extracytoplasmic proteins containing more than one cysteine residue often require introduction of disulfide bonds. This process takes place in an oxidative environment, such as the periplasm of Gram-negative bacteria, and is catalyzed by Dsb (disulfide bond formation) proteins. Mutations in dsb genes influence the conformation and stability of many extracytoplasmic proteins. Thus, many pathogens become partially or fully attenuated due to improper folding of proteins that act as virulence factors. This review summarizes the current knowledge on Dsb proteins and their effect on the pathogenicity of Gram-negative bacteria. The potential application of Dsb proteins in biotechnology is also discussed.
MeSH term(s)	Bacterial Proteins/metabolism ; Gram-Negative Bacteria/chemistry ; Gram-Negative Bacteria/pathogenicity ; Membrane Proteins/metabolism ; Protein Folding ; Virulence Factors/metabolism
Chemical Substances	Bacterial Proteins ; Membrane Proteins ; Virulence Factors
Language	English
Publishing date	2007-09
Publishing country	England
Document type	Journal Article ; Review
ZDB-ID	283740-7
ISSN	1574-6976 ; 0168-6445
ISSN (online)	1574-6976
ISSN	0168-6445
DOI	10.1111/j.1574-6976.2007.00081.x
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Article: The role of Dsb proteins of Gram-negative bacteria in the process of pathogenesis

Łasica, Anna M / Jagusztyn-Krynicka, Elżbieta K

FEMS microbiology reviews. 2007 Sept., v. 31, no. 5

2007

Abstract	Tertiary and quaternary structures of extracytoplasmic proteins containing more than one cysteine residue often require introduction of disulfide bonds. This process takes place in an oxidative environment, such as the periplasm of Gram-negative bacteria, and is catalyzed by Dsb (disulfide bond formation) proteins. Mutations in dsb genes influence the conformation and stability of many extracytoplasmic proteins. Thus, many pathogens become partially or fully attenuated due to improper folding of proteins that act as virulence factors. This review summarizes the current knowledge on Dsb proteins and their effect on the pathogenicity of Gram-negative bacteria. The potential application of Dsb proteins in biotechnology is also discussed.
Keywords	protein folding ; pathogenesis ; virulence
Language	English
Dates of publication	2007-09
Size	p. 626-636.
Publisher	Blackwell Publishing Ltd
Publishing place	Oxford, UK
Document type	Article
ZDB-ID	283740-7
ISSN	1574-6976 ; 0168-6445
ISSN (online)	1574-6976
ISSN	0168-6445
DOI	10.1111/j.1574-6976.2007.00081.x
Database	NAL-Catalogue (AGRICOLA)

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