LIVIVO - Search results -

Search results

Result 1 - 10 of total 32

Search options

Article ; Online: Curli Biogenesis: Bacterial Amyloid Assembly by the Type VIII Secretion Pathway.

Bhoite, Sujeet / van Gerven, Nani / Chapman, Matthew R / Remaut, Han

EcoSal Plus

2019 Volume 8, Issue 2

Abstract: In 1989, Normark and coworkers reported on fibrous surface structures called curli on strains ... ...

Abstract	In 1989, Normark and coworkers reported on fibrous surface structures called curli on strains of
MeSH term(s)	Amyloid/chemistry ; Amyloidogenic Proteins/chemistry ; Bacteria/chemistry ; Bacterial Proteins/chemistry ; Escherichia coli/chemistry ; Escherichia coli Proteins/chemistry ; Organelle Biogenesis ; Secretory Pathway
Chemical Substances	Amyloid ; Amyloidogenic Proteins ; Bacterial Proteins ; Escherichia coli Proteins ; Crl protein, Bacteria (148349-72-8)
Language	English
Publishing date	2019-04-17
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ISSN	2324-6200
ISSN (online)	2324-6200
DOI	10.1128/ecosalplus.ESP-0037-2018
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

Inter-library loan at ZB MED

Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

Article ; Online: Nucleation of protein mesocrystals via oriented attachment.

Van Driessche, Alexander E S / Van Gerven, Nani / Joosten, Rick R M / Ling, Wai Li / Bacia, Maria / Sommerdijk, Nico / Sleutel, Mike

Nature communications

2021 Volume 12, Issue 1, Page(s) 3902

Abstract: Self-assembly of proteins holds great promise for the bottom-up design and production of synthetic biomaterials. In conventional approaches, designer proteins are pre-programmed with specific recognition sites that drive the association process towards a ...

Abstract	Self-assembly of proteins holds great promise for the bottom-up design and production of synthetic biomaterials. In conventional approaches, designer proteins are pre-programmed with specific recognition sites that drive the association process towards a desired organized state. Although proven effective, this approach poses restrictions on the complexity and material properties of the end-state. An alternative, hierarchical approach that has found wide adoption for inorganic systems, relies on the production of crystalline nanoparticles that become the building blocks of a next-level assembly process driven by oriented attachment (OA). As it stands, OA has not yet been observed for protein systems. Here we employ cryo-transmission electron microscopy (cryoEM) in the high nucleation rate limit of protein crystals and map the self-assembly route at molecular resolution. We observe the initial formation of facetted nanocrystals that merge lattices by means of OA alignment well before contact is made, satisfying non-trivial symmetry rules in the process. As these nanocrystalline assemblies grow larger we witness imperfect docking events leading to oriented aggregation into mesocrystalline assemblies. These observations highlight the underappreciated role of the interaction between crystalline nuclei, and the impact of OA on the crystallization process of proteins.
MeSH term(s)	Aldose-Ketose Isomerases/chemistry ; Aldose-Ketose Isomerases/genetics ; Aldose-Ketose Isomerases/metabolism ; Cryoelectron Microscopy ; Crystallization ; Crystallography, X-Ray ; Kinetics ; Models, Molecular ; Nanostructures/chemistry ; Nanostructures/ultrastructure ; Particle Size ; Point Mutation ; Recombinant Proteins/chemistry ; Recombinant Proteins/metabolism ; Recombinant Proteins/ultrastructure
Chemical Substances	Recombinant Proteins ; Aldose-Ketose Isomerases (EC 5.3.1.-) ; xylose isomerase (EC 5.3.1.5)
Language	English
Publishing date	2021-06-23
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2553671-0
ISSN	2041-1723 ; 2041-1723
ISSN (online)	2041-1723
ISSN	2041-1723
DOI	10.1038/s41467-021-24171-z
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Article: The Role of Functional Amyloids in Bacterial Virulence

Van Gerven, Nani / Van der Verren, Sander E / Reiter, Dirk M / Remaut, Han

Journal of molecular biology. 2018 Oct. 12, v. 430, no. 20

2018

Abstract: Amyloid fibrils are best known as a product of human and animal protein misfolding disorders, where amyloid formation is associated with cytotoxicity and disease. It is now evident that for some proteins, the amyloid state constitutes the native ... ...

Abstract	Amyloid fibrils are best known as a product of human and animal protein misfolding disorders, where amyloid formation is associated with cytotoxicity and disease. It is now evident that for some proteins, the amyloid state constitutes the native structure and serves a functional role. These functional amyloids are proving widespread in bacteria and fungi, fulfilling diverse functions as structural components in biofilms or spore coats, as toxins and surface-active fibers, as epigenetic material, peptide reservoirs or adhesins mediating binding to and internalization into host cells. In this review, we will focus on the role of functional amyloids in bacterial pathogenesis. The role of functional amyloids as virulence factor is diverse but mostly indirect. Nevertheless, functional amyloid pathways deserve consideration for the acute and long-term effects of the infectious disease process and may form valid antimicrobial targets.
Keywords	adhesins ; amyloid ; animal proteins ; bacteria ; biofilm ; cytotoxicity ; epigenetics ; fungi ; humans ; infectious diseases ; long term effects ; pathogenesis ; protein folding ; spores ; toxins ; virulence
Language	English
Dates of publication	2018-1012
Size	p. 3657-3684.
Publishing place	Elsevier Ltd
Document type	Article
ZDB-ID	80229-3
ISSN	1089-8638 ; 0022-2836
ISSN (online)	1089-8638
ISSN	0022-2836
DOI	10.1016/j.jmb.2018.07.010
Database	NAL-Catalogue (AGRICOLA)

In stock of ZB MED Bonn / Germany

Z 4' 63/108: Show issues

Order via subito

Inter-library loan at ZB MED

Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: Nucleation of protein mesocrystals via oriented attachment

Alexander E. S. Van Driessche / Nani Van Gerven / Rick R. M. Joosten / Wai Li Ling / Maria Bacia / Nico Sommerdijk / Mike Sleutel

Nature Communications, Vol 12, Iss 1, Pp 1-

2021 Volume 8

Abstract: Past studies on protein nucleation have focused on the routes that molecules follow towards a crystalline cluster, while possible interactions that may occur between nuclei have not been investigated. Here, the authors show that in the high ... ...

Abstract	Past studies on protein nucleation have focused on the routes that molecules follow towards a crystalline cluster, while possible interactions that may occur between nuclei have not been investigated. Here, the authors show that in the high supersaturation limit such interactions dominate the nucleation process in the form of inter-nucleus docking driving by oriented attachment.
Keywords	Science ; Q
Language	English
Publishing date	2021-06-01T00:00:00Z
Publisher	Nature Portfolio
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

Full text online

Full text

Inter-library loan at ZB MED

Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

Article ; Online: The Role of Functional Amyloids in Bacterial Virulence.

Van Gerven, Nani / Van der Verren, Sander E / Reiter, Dirk M / Remaut, Han

Journal of molecular biology

2018 Volume 430, Issue 20, Page(s) 3657–3684

Abstract	Amyloid fibrils are best known as a product of human and animal protein misfolding disorders, where amyloid formation is associated with cytotoxicity and disease. It is now evident that for some proteins, the amyloid state constitutes the native structure and serves a functional role. These functional amyloids are proving widespread in bacteria and fungi, fulfilling diverse functions as structural components in biofilms or spore coats, as toxins and surface-active fibers, as epigenetic material, peptide reservoirs or adhesins mediating binding to and internalization into host cells. In this review, we will focus on the role of functional amyloids in bacterial pathogenesis. The role of functional amyloids as virulence factor is diverse but mostly indirect. Nevertheless, functional amyloid pathways deserve consideration for the acute and long-term effects of the infectious disease process and may form valid antimicrobial targets.
MeSH term(s)	Amyloid/chemistry ; Amyloid/metabolism ; Amyloid/ultrastructure ; Amyloidosis/etiology ; Amyloidosis/metabolism ; Animals ; Antigens/immunology ; Antigens/metabolism ; Bacteria/genetics ; Bacteria/metabolism ; Bacteria/pathogenicity ; Bacteria/ultrastructure ; Bacterial Infections/microbiology ; Bacterial Proteins/chemistry ; Bacterial Proteins/genetics ; Bacterial Proteins/metabolism ; Biofilms ; Humans ; Protein Multimerization ; Toxins, Biological/immunology ; Toxins, Biological/metabolism ; Virulence
Chemical Substances	Amyloid ; Antigens ; Bacterial Proteins ; Toxins, Biological ; Crl protein, Bacteria (148349-72-8)
Language	English
Publishing date	2018-07-12
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	80229-3
ISSN	1089-8638 ; 0022-2836
ISSN (online)	1089-8638
ISSN	0022-2836
DOI	10.1016/j.jmb.2018.07.010
Database	MEDical Literature Analysis and Retrieval System OnLINE

Full text online

Accessible to users with ZB MED library card

In stock of ZB MED Cologne/Königswinter

Zs.A 867: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
Jg. 1995 - 2021: Lesesall (1.OG)
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾

Article ; Online: Bacterial amyloid formation: structural insights into curli biogensis.

Van Gerven, Nani / Klein, Roger D / Hultgren, Scott J / Remaut, Han

Trends in microbiology

2015 Volume 23, Issue 11, Page(s) 693–706

Abstract: Curli are functional amyloid fibers assembled by many Gram-negative bacteria as part of an extracellular matrix that encapsulates the bacteria within a biofilm. A multicomponent secretion system ensures the safe transport of the aggregation-prone curli ... ...

Abstract	Curli are functional amyloid fibers assembled by many Gram-negative bacteria as part of an extracellular matrix that encapsulates the bacteria within a biofilm. A multicomponent secretion system ensures the safe transport of the aggregation-prone curli subunits across the periplasm and outer membrane, and coordinates subunit self-assembly into surface-attached fibers. To avoid the build-up of potentially toxic intracellular protein aggregates, the timing and location of the interactions of the different curli proteins are of paramount importance. Here we review the structural and molecular biology of curli biogenesis, with a focus on the recent breakthroughs in our understanding of subunit chaperoning and secretion. The mechanistic insight into the curli assembly pathway will provide tools for new biotechnological applications and inform the design of targeted inhibitors of amyloid polymerization and biofilm formation.
MeSH term(s)	Amyloid/antagonists & inhibitors ; Amyloid/biosynthesis ; Amyloid/metabolism ; Bacterial Proteins/biosynthesis ; Bacterial Proteins/metabolism ; Biofilms/growth & development ; Escherichia coli/metabolism ; Escherichia coli Proteins/metabolism ; Molecular Chaperones/metabolism
Chemical Substances	Amyloid ; Bacterial Proteins ; Escherichia coli Proteins ; Molecular Chaperones ; Crl protein, Bacteria (148349-72-8)
Language	English
Publishing date	2015-10-01
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	1158963-2
ISSN	1878-4380 ; 0966-842X
ISSN (online)	1878-4380
ISSN	0966-842X
DOI	10.1016/j.tim.2015.07.010
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 3738: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
Jg. 1995 - 2021: Lesesall (2.OG)
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: A dual-constriction biological nanopore resolves homonucleotide sequences with high fidelity.

Van der Verren, Sander E / Van Gerven, Nani / Jonckheere, Wim / Hambley, Richard / Singh, Pratik / Kilgour, John / Jordan, Michael / Wallace, E Jayne / Jayasinghe, Lakmal / Remaut, Han

Nature biotechnology

2020 Volume 38, Issue 12, Page(s) 1415–1420

Abstract: Single-molecule long-read DNA sequencing with biological nanopores is fast and high-throughput but suffers reduced accuracy in homonucleotide stretches. We now combine the CsgG nanopore with the 35-residue N-terminal region of its extracellular ... ...

Abstract	Single-molecule long-read DNA sequencing with biological nanopores is fast and high-throughput but suffers reduced accuracy in homonucleotide stretches. We now combine the CsgG nanopore with the 35-residue N-terminal region of its extracellular interaction partner CsgF to produce a dual-constriction pore with improved signal and base-calling accuracy for homopolymer regions. The electron cryo-microscopy structure of CsgG in complex with full-length CsgF shows that the 33 N-terminal residues of CsgF bind inside the β-barrel of the pore, forming a defined second constriction. In complexes of CsgG bound to a 35-residue CsgF constriction peptide, the second constriction is separated from the primary constriction by ~25 Å. We find that both constrictions contribute to electrical signal modulation during single-stranded DNA translocation. DNA sequencing using a prototype CsgG-CsgF protein pore with two constrictions improved single-read accuracy by 25 to 70% in homopolymers up to 9 nucleotides long.
MeSH term(s)	Base Sequence ; Cryoelectron Microscopy ; DNA/metabolism ; Escherichia coli Proteins/chemistry ; Escherichia coli Proteins/metabolism ; Escherichia coli Proteins/ultrastructure ; Models, Molecular ; Nanopores ; Nucleotides/genetics
Chemical Substances	Escherichia coli Proteins ; Nucleotides ; DNA (9007-49-2)
Language	English
Publishing date	2020-07-06
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1311932-1
ISSN	1546-1696 ; 1087-0156
ISSN (online)	1546-1696
ISSN	1087-0156
DOI	10.1038/s41587-020-0570-8
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 2167: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (1.OG) ab Jg. 2022: Lesesaal (EG)
Zs.MO 137: Show issues
Zs.MG 43: Show issues

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article: Bacterial Amyloid Formation: Structural Insights into Curli Biogensis

Van Gerven, Nani / Klein, Roger D / Hultgren, Scott J / Remaut, Han

Elsevier Ltd Trends in microbiology. 2015 Nov., v. 23

2015

Abstract	Curli are functional amyloid fibers assembled by many Gram-negative bacteria as part of an extracellular matrix that encapsulates the bacteria within a biofilm. A multicomponent secretion system ensures the safe transport of the aggregation-prone curli subunits across the periplasm and outer membrane, and coordinates subunit self-assembly into surface-attached fibers. To avoid the build-up of potentially toxic intracellular protein aggregates, the timing and location of the interactions of the different curli proteins are of paramount importance. Here we review the structural and molecular biology of curli biogenesis, with a focus on the recent breakthroughs in our understanding of subunit chaperoning and secretion. The mechanistic insight into the curli assembly pathway will provide tools for new biotechnological applications and inform the design of targeted inhibitors of amyloid polymerization and biofilm formation.
Keywords	Gram-negative bacteria ; amyloid ; biofilm ; biogenesis ; extracellular matrix ; molecular biology ; polymerization ; protein aggregates ; secretion ; toxicity
Language	English
Dates of publication	2015-11
Size	p. 693-706.
Publishing place	Elsevier Ltd
Document type	Article
ZDB-ID	1158963-2
ISSN	1878-4380 ; 0966-842X
ISSN (online)	1878-4380
ISSN	0966-842X
DOI	10.1016/j.tim.2015.07.010
Database	NAL-Catalogue (AGRICOLA)

In stock of ZB MED Bonn / Germany

Z 2005/714: Show issues

Order via subito

Inter-library loan at ZB MED

Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: Crystallization and preliminary X-ray crystallographic analysis of the curli transporter CsgG.

Goyal, Parveen / Van Gerven, Nani / Jonckheere, Wim / Remaut, Han

Acta crystallographica. Section F, Structural biology and crystallization communications

2013 Volume 69, Issue Pt 12, Page(s) 1349–1353

Abstract: Gram-negative bacteria have eight known protein secretion systems. The type-VIII secretion system, also known as the curli biosynthesis system, is responsible for the formation of aggregative fibres known in Escherichia coli as curli. Curli are ... ...

Abstract	Gram-negative bacteria have eight known protein secretion systems. The type-VIII secretion system, also known as the curli biosynthesis system, is responsible for the formation of aggregative fibres known in Escherichia coli as curli. Curli are extracellular proteinaceous fibres primarily involved in bacterial biofilm formation and attachment to nonbiotic surfaces. The secretion of curli subunits depends on a dedicated lipoprotein, CsgG, which is found to form an oligomeric secretion channel in the outer membrane. A nonlipidated mutant of CsgG was expressed and crystallized in a soluble form. The crystals diffracted to 3.15 Å resolution and belong to space group P1 with a unit cell containing a predicted 16 molecules per asymmetric unit.
MeSH term(s)	Crystallization ; Crystallography, X-Ray ; Escherichia coli/chemistry ; Escherichia coli/genetics ; Escherichia coli Proteins/chemistry ; Escherichia coli Proteins/isolation & purification ; Gene Expression ; Lipoproteins/chemistry ; Lipoproteins/isolation & purification ; Protein Multimerization ; Recombinant Proteins/chemistry ; Recombinant Proteins/isolation & purification
Chemical Substances	CsgG protein, E coli ; Escherichia coli Proteins ; Lipoproteins ; Recombinant Proteins
Language	English
Publishing date	2013-11-28
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	1744-3091
ISSN (online)	1744-3091
DOI	10.1107/S1744309113028054
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Inter-library loan at ZB MED

Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

Article ; Online: Pili and flagella biology, structure, and biotechnological applications.

Van Gerven, Nani / Waksman, Gabriel / Remaut, Han

Progress in molecular biology and translational science

2011 Volume 103, Page(s) 21–72

Abstract: Bacteria and Archaea expose on their outer surfaces a variety of thread-like proteinaceous organelles with which they interact with their environments. These structures are repetitive assemblies of covalently or non-covalently linked protein subunits, ... ...

Abstract	Bacteria and Archaea expose on their outer surfaces a variety of thread-like proteinaceous organelles with which they interact with their environments. These structures are repetitive assemblies of covalently or non-covalently linked protein subunits, organized into filamentous polymers known as pili ("hair"), flagella ("whips") or injectisomes ("needles"). They serve different roles in cell motility, adhesion and host invasion, protein and DNA secretion and uptake, conductance, or cellular encapsulation. Here we describe the functional, morphological and genetic diversity of these bacterial filamentous protein structures. The organized, multi-copy build-up and/or the natural function of pili and flagella have lead to their biotechnological application as display and secretion tools, as therapeutic targets or as molecular motors. We review the documented and potential technological exploitation of bacterial surface filaments in light of their structural and functional traits.
MeSH term(s)	Archaea/metabolism ; Bacterial Proteins/metabolism ; Biotechnology/methods ; Fimbriae, Bacterial/chemistry ; Fimbriae, Bacterial/metabolism ; Flagella/chemistry ; Flagella/metabolism ; Organelles/metabolism
Chemical Substances	Bacterial Proteins
Language	English
Publishing date	2011-06-28
Publishing country	Netherlands
Document type	Journal Article ; Review
ZDB-ID	2471995-X
ISSN	1878-0814 ; 0079-6603 ; 1877-1173
ISSN (online)	1878-0814
ISSN	0079-6603 ; 1877-1173
DOI	10.1016/B978-0-12-415906-8.00005-4
Database	MEDical Literature Analysis and Retrieval System OnLINE

Full text online

Accessible to users with ZB MED library card

In stock of ZB MED Cologne/Königswinter

Uc I Zs 357: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾

To top

More links

Kategorien

Order via subito

Inter-library loan at ZB MED

More links

Kategorien

Order via subito

More links

Kategorien

In stock of ZB MED Bonn / Germany

Order via subito

Inter-library loan at ZB MED

Full text online

More links

Kategorien

Inter-library loan at ZB MED

Full text online

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

In stock of ZB MED Bonn / Germany

Order via subito

Inter-library loan at ZB MED

More links

Kategorien

Order via subito

Inter-library loan at ZB MED

Full text online

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito