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Article ; Online: Mechanism of assembly of type 4 filaments: everything you always wanted to know (but were afraid to ask).

Pelicic, Vladimir

2023 Volume 169, Issue 3

Abstract: Type 4 filaments (T4F) are a superfamily of filamentous nanomachines - virtually ubiquitous in prokaryotes and functionally versatile - of which type 4 pili (T4P) are the defining member. T4F are polymers of type 4 pilins, assembled by conserved multi- ... ...

Abstract	Type 4 filaments (T4F) are a superfamily of filamentous nanomachines - virtually ubiquitous in prokaryotes and functionally versatile - of which type 4 pili (T4P) are the defining member. T4F are polymers of type 4 pilins, assembled by conserved multi-protein machineries. They have long been an important topic for research because they are key virulence factors in numerous bacterial pathogens. Our poor understanding of the molecular mechanisms of T4F assembly is a serious hindrance to the design of anti-T4F therapeutics. This review attempts to shed light on the fundamental mechanistic principles at play in T4F assembly by focusing on similarities rather than differences between several (mostly bacterial) T4F. This holistic approach, complemented by the revolutionary ability of artificial intelligence to predict protein structures, led to an intriguing mechanistic model of T4F assembly.
MeSH term(s)	Artificial Intelligence ; Fimbriae Proteins/metabolism ; Fimbriae, Bacterial/genetics ; Fimbriae, Bacterial/metabolism ; Bacteria/genetics ; Bacteria/metabolism ; Virulence Factors/metabolism
Chemical Substances	Fimbriae Proteins (147680-16-8) ; Virulence Factors
Language	English
Publishing date	2023-03-22
Publishing country	England
Document type	Review ; Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1180712-x
ISSN	1465-2080 ; 1350-0872
ISSN (online)	1465-2080
ISSN	1350-0872
DOI	10.1099/mic.0.001311
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Article ; Online: Monoderm bacteria: the new frontier for type IV pilus biology.

Pelicic, Vladimir

Molecular microbiology

2019 Volume 112, Issue 6, Page(s) 1674–1683

Abstract: In the diverse world of bacterial pili, type IV pili (Tfp) are unique for two reasons: their multifunctionality and ubiquity. This latter feature offers an extraordinary possibility, that is, to perform comparative studies in evolutionarily distant ... ...

Abstract	In the diverse world of bacterial pili, type IV pili (Tfp) are unique for two reasons: their multifunctionality and ubiquity. This latter feature offers an extraordinary possibility, that is, to perform comparative studies in evolutionarily distant species in order to improve our fragmentary understanding of Tfp biology. Regrettably, such potential has remained largely untapped, because, for 20 years, Tfp have only been characterised in diderm bacteria. However, recent studies of Tfp in monoderms have started closing the gap, revealing many interesting commonalities and a few significant differences, extending the frontiers of knowledge of Tfp biology. Here, I review the current state of the art of the Tfp field in monoderm bacteria and discuss resulting implications for our general understanding of the assembly and function of these widespread filamentous nanomachines.
MeSH term(s)	Bacteria ; Bacterial Proteins ; Clostridiales ; Fimbriae Proteins/genetics ; Fimbriae Proteins/metabolism ; Fimbriae, Bacterial/genetics ; Fimbriae, Bacterial/metabolism ; Gram-Positive Bacteria/genetics ; Gram-Positive Bacteria/metabolism ; Membrane Proteins/metabolism ; Streptococcus ; Streptococcus sanguis
Chemical Substances	Bacterial Proteins ; Membrane Proteins ; Fimbriae Proteins (147680-16-8)
Language	English
Publishing date	2019-10-08
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	619315-8
ISSN	1365-2958 ; 0950-382X
ISSN (online)	1365-2958
ISSN	0950-382X
DOI	10.1111/mmi.14397
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Article ; Online: Development of maxillofacial traumatology and review of the epidemiology and quality of life of patients with facial bone fractures

Boljević Tanja V. / Peličić Damir N. / Vojinović Tanja B.

Hospital Pharmacology, Vol 10, Iss 2, Pp 1276-

2023 Volume 1284

Abstract: Introduction: The treatment of facial bone fractures dates back to ancient civilizations, with various methods of prosthetic immobilization developed and in the second half of the 19th and the beginning of the 20th century. In our literature, there are ... ...

Abstract	Introduction: The treatment of facial bone fractures dates back to ancient civilizations, with various methods of prosthetic immobilization developed and in the second half of the 19th and the beginning of the 20th century. In our literature, there are almost no studies that examined the quality of life of patients with facial bone fractures, although worldwide this is an extremely current topic indicating the importance of this problem. Methods: This paper will present results from professional/scientific relevant data sources on the historical development of maxillofacial surgery with reference to etiology, epidemiology and instruments for assessing the quality of life of patients with jaw bone fractures. Topic: Medical treatment of these surgical injuries involves a highly specialized team led by a maxillofacial surgeon. This paper deals with the etiology, epidemiology and quality of life of patients with facial bone fractures. Conclusion: Surgical interventions for fractures of the facial bones are becoming more and more demanding, resulting in development of maxillofacial surgery as an independent branch. In the etiology of facial bone fractures, traffic accidents are mentioned more and more often as the main way of injury. The incidence of facial bone fractures in human pathology is about 30 per 100,000 hospitalized patients. Research has shown that the quality of life in operated patients with fractures of the facial bones is significantly lower than those operated on some other region.
Keywords	maxillofacial surgery ; history of medicine ; trauma ; quality of life ; fractures facial bones ; Therapeutics. Pharmacology ; RM1-950
Subject code	616
Language	English
Publishing date	2023-01-01T00:00:00Z
Publisher	Srpsko lekarsko drustvo
Document type	Article ; Online
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Article ; Online: Systematic functional analysis of the Com pilus in

Mom, Jeremy / Chouikha, Iman / Valette, Odile / Pieulle, Laetitia / Pelicic, Vladimir

mBio

2023 Volume 15, Issue 1, Page(s) e0266723

Abstract: Importance: Type 4 filaments (T4F) are nanomachines ubiquitous in prokaryotes, centered on filamentous polymers of type 4 pilins. T4F are exceptionally versatile and widespread virulence factors in bacterial pathogens. The mechanisms of filament ... ...

Abstract	Importance: Type 4 filaments (T4F) are nanomachines ubiquitous in prokaryotes, centered on filamentous polymers of type 4 pilins. T4F are exceptionally versatile and widespread virulence factors in bacterial pathogens. The mechanisms of filament assembly and the many functions they facilitate remain poorly understood because of the complexity of T4F machineries. This hinders the development of anti-T4F drugs. The significance of our research lies in characterizing the simplest known T4F-the Com pilus that mediates DNA uptake in competent monoderm bacteria-and showing that four protein components universally conserved in T4F are sufficient for filament assembly. The Com pilus becomes a model for elucidating the mechanisms of T4F assembly.
MeSH term(s)	Streptococcus sanguis/genetics ; Streptococcus sanguis/metabolism ; Fimbriae, Bacterial/genetics ; Fimbriae, Bacterial/metabolism ; Bacteria/genetics ; Fimbriae Proteins/genetics ; Fimbriae Proteins/metabolism ; DNA/metabolism
Chemical Substances	Fimbriae Proteins (147680-16-8) ; DNA (9007-49-2)
Language	English
Publishing date	2023-12-14
Publishing country	United States
Document type	Journal Article
ZDB-ID	2557172-2
ISSN	2150-7511 ; 2161-2129
ISSN (online)	2150-7511
ISSN	2161-2129
DOI	10.1128/mbio.02667-23
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Article ; Online: Characterization of a glycan-binding complex of minor pilins completes the analysis of

Shahin, Meriam / Sheppard, Devon / Raynaud, Claire / Berry, Jamie-Lee / Gurung, Ishwori / Silva, Lisete M / Feizi, Ten / Liu, Yan / Pelicic, Vladimir

Proceedings of the National Academy of Sciences of the United States of America

2023 Volume 120, Issue 3, Page(s) e2216237120

Abstract: Type 4 filaments (T4F)-of which type 4 pili (T4P) are the archetype-are a superfamily of nanomachines nearly ubiquitous in prokaryotes. T4F are polymers of one major pilin, which also contain minor pilins whose roles are often poorly understood. Here, we ...

Abstract	Type 4 filaments (T4F)-of which type 4 pili (T4P) are the archetype-are a superfamily of nanomachines nearly ubiquitous in prokaryotes. T4F are polymers of one major pilin, which also contain minor pilins whose roles are often poorly understood. Here, we complete the structure/function analysis of the full set of T4P pilins in the opportunistic bacterial pathogen
MeSH term(s)	Humans ; Fimbriae Proteins/genetics ; Fimbriae Proteins/chemistry ; Streptococcus sanguis ; Fimbriae, Bacterial/metabolism
Chemical Substances	Fimbriae Proteins (147680-16-8)
Language	English
Publishing date	2023-01-10
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	209104-5
ISSN	1091-6490 ; 0027-8424
ISSN (online)	1091-6490
ISSN	0027-8424
DOI	10.1073/pnas.2216237120
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Article ; Online: Structure of a heteropolymeric type 4 pilus from a monoderm bacterium.

Anger, Robin / Pieulle, Laetitia / Shahin, Meriam / Valette, Odile / Le Guenno, Hugo / Kosta, Artemis / Pelicic, Vladimir / Fronzes, Rémi

Nature communications

2023 Volume 14, Issue 1, Page(s) 7143

Abstract: Type 4 pili (T4P) are important virulence factors, which belong to a superfamily of nanomachines ubiquitous in prokaryotes, called type 4 filaments (T4F). T4F are defined as helical polymers of type 4 pilins. Recent advances in cryo-electron microscopy ( ... ...

Abstract	Type 4 pili (T4P) are important virulence factors, which belong to a superfamily of nanomachines ubiquitous in prokaryotes, called type 4 filaments (T4F). T4F are defined as helical polymers of type 4 pilins. Recent advances in cryo-electron microscopy (cryo-EM) led to structures of several T4F, revealing that the long N-terminal α-helix (α1) - the trademark of pilins - packs in the centre of the filaments to form a hydrophobic core. In diderm bacteria - all available bacterial T4F structures are from diderm species - a portion of α1 is melted (unfolded). Here we report that this architecture is conserved in phylogenetically distant monoderm species by determining the structure of Streptococcus sanguinis T4P. Our 3.7 Å resolution cryo-EM structure of S. sanguinis heteropolymeric T4P and the resulting full atomic model including all minor pilins highlight universal features of bacterial T4F and have widespread implications in understanding T4F biology.
MeSH term(s)	Fimbriae Proteins/chemistry ; Cryoelectron Microscopy/methods ; Fimbriae, Bacterial/chemistry ; Bacteria ; Polymers
Chemical Substances	Fimbriae Proteins (147680-16-8) ; Polymers
Language	English
Publishing date	2023-11-06
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/s41467-023-42872-5
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Article ; Online: Type IV pili: e pluribus unum?

Pelicic, Vladimir

Molecular microbiology

2008 Volume 68, Issue 4, Page(s) 827–837

Abstract: The widespread role of pili as colonization factors in pathogens has long been recognized in Gram-negative bacteria and more recently in Gram-positive bacteria, making the study of these hair-like filaments a perennial hot topic for research. No other ... ...

Abstract	The widespread role of pili as colonization factors in pathogens has long been recognized in Gram-negative bacteria and more recently in Gram-positive bacteria, making the study of these hair-like filaments a perennial hot topic for research. No other pili are found in as many or as diverse bacteria as type IV pili. This is likely a consequence of their ancient origin and unique ability to promote multiple and strikingly different phenotypes such as attachment to surfaces, aggregation, uptake of DNA during transformation, motility, etc. Two decades of investigations in several model species have shed some light on the structure of these filaments and the molecular basis of some of the properties they confer. Moreover, recent discoveries have led to a better knowledge of the genetic basis and molecular mechanisms of type IV pili biogenesis. This brings us a few steps closer to understanding how these filaments are produced, but leaves us wondering whether (as in the famous motto that inspired the title) out of the many models studied will emerge one unifying mechanism.
MeSH term(s)	Cell Membrane/metabolism ; Fimbriae Proteins/metabolism ; Fimbriae, Bacterial/classification ; Fimbriae, Bacterial/metabolism ; Gram-Negative Bacteria/cytology ; Gram-Negative Bacteria/physiology ; Gram-Positive Bacteria/cytology ; Gram-Positive Bacteria/physiology
Chemical Substances	Fimbriae Proteins (147680-16-8)
Language	English
Publishing date	2008-04-08
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	619315-8
ISSN	1365-2958 ; 0950-382X
ISSN (online)	1365-2958
ISSN	0950-382X
DOI	10.1111/j.1365-2958.2008.06197.x
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Article ; Online: PilB from

Raynaud, Claire / Sheppard, Devon / Berry, Jamie-Lee / Gurung, Ishwori / Pelicic, Vladimir

Proceedings of the National Academy of Sciences of the United States of America

2021 Volume 118, Issue 22

Abstract: Type IV pili (T4P) are functionally versatile filamentous nanomachines, nearly ubiquitous in prokaryotes. They are predominantly polymers of one major pilin but also contain minor pilins whose functions are often poorly defined and likely to be diverse. ... ...

Abstract	Type IV pili (T4P) are functionally versatile filamentous nanomachines, nearly ubiquitous in prokaryotes. They are predominantly polymers of one major pilin but also contain minor pilins whose functions are often poorly defined and likely to be diverse. Here, we show that the minor pilin PilB from the T4P of
MeSH term(s)	Amino Acid Sequence ; Animals ; Bacterial Proteins/chemistry ; Bacterial Proteins/physiology ; CHO Cells ; Cell Adhesion ; Cricetulus ; Escherichia coli ; Fimbriae Proteins/chemistry ; Fimbriae Proteins/physiology ; Humans ; Oxidoreductases/chemistry ; Oxidoreductases/physiology ; Protein Conformation ; Streptococcus sanguis/chemistry ; Streptococcus sanguis/physiology
Chemical Substances	Bacterial Proteins ; Fimbriae Proteins (147680-16-8) ; Oxidoreductases (EC 1.-) ; pilB protein, Bacteria (EC 1.8.4.13)
Language	English
Publishing date	2021-05-24
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	209104-5
ISSN	1091-6490 ; 0027-8424
ISSN (online)	1091-6490
ISSN	0027-8424
DOI	10.1073/pnas.2102092118
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Article ; Online: The major subunit of widespread competence pili exhibits a novel and conserved type IV pilin fold.

Sheppard, Devon / Berry, Jamie-Lee / Denise, Rémi / Rocha, Eduardo P C / Matthews, Steve / Pelicic, Vladimir

The Journal of biological chemistry

2020 Volume 295, Issue 19, Page(s) 6594–6604

Abstract: Type IV filaments (T4F), which are helical assemblies of type IV pilins, constitute a superfamily of filamentous nanomachines virtually ubiquitous in prokaryotes that mediate a wide variety of functions. The competence (Com) pilus is a widespread T4F, ... ...

Abstract	Type IV filaments (T4F), which are helical assemblies of type IV pilins, constitute a superfamily of filamentous nanomachines virtually ubiquitous in prokaryotes that mediate a wide variety of functions. The competence (Com) pilus is a widespread T4F, mediating DNA uptake (the first step in natural transformation) in bacteria with one membrane (monoderms), an important mechanism of horizontal gene transfer. Here, we report the results of genomic, phylogenetic, and structural analyses of ComGC, the major pilin subunit of Com pili. By performing a global comparative analysis, we show that Com pili genes are virtually ubiquitous in Bacilli, a major monoderm class of Firmicutes. This also revealed that ComGC displays extensive sequence conservation, defining a monophyletic group among type IV pilins. We further report ComGC solution structures from two naturally competent human pathogens,
MeSH term(s)	Fimbriae Proteins/chemistry ; Fimbriae Proteins/genetics ; Fimbriae, Bacterial/chemistry ; Fimbriae, Bacterial/genetics ; Protein Folding ; Streptococcus pneumoniae/chemistry ; Streptococcus pneumoniae/genetics ; Streptococcus sanguis/chemistry ; Streptococcus sanguis/genetics
Chemical Substances	Fimbriae Proteins (147680-16-8)
Language	English
Publishing date	2020-04-09
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1074/jbc.RA120.013316
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Article ; Online: Construction of a complete set of Neisseria meningitidis mutants and its use for the phenotypic profiling of this human pathogen.

Muir, Alastair / Gurung, Ishwori / Cehovin, Ana / Bazin, Adelme / Vallenet, David / Pelicic, Vladimir

Nature communications

2020 Volume 11, Issue 1, Page(s) 5541

Abstract: The bacterium Neisseria meningitidis causes life-threatening meningitis and sepsis. Here, we construct a complete collection of defined mutants in protein-coding genes of this organism, identifying all genes that are essential under laboratory conditions. ...

Abstract	The bacterium Neisseria meningitidis causes life-threatening meningitis and sepsis. Here, we construct a complete collection of defined mutants in protein-coding genes of this organism, identifying all genes that are essential under laboratory conditions. The collection, named NeMeSys 2.0, consists of individual mutants in 1584 non-essential genes. We identify 391 essential genes, which are associated with basic functions such as expression and preservation of genome information, cell membrane structure and function, and metabolism. We use this collection to shed light on the functions of diverse genes, including a gene encoding a member of a previously unrecognised class of histidinol-phosphatases; a set of 20 genes required for type IV pili function; and several conditionally essential genes encoding antitoxins and/or immunity proteins. We expect that NeMeSys 2.0 will facilitate the phenotypic profiling of a major human bacterial pathogen.
MeSH term(s)	Bacterial Proteins/metabolism ; Computational Biology ; Fimbriae Proteins/genetics ; Fimbriae Proteins/metabolism ; Fimbriae, Bacterial/genetics ; Fimbriae, Bacterial/metabolism ; Gene Expression Profiling ; Gene Expression Regulation, Bacterial ; Genes, Bacterial/genetics ; Genes, Essential/genetics ; Genome, Bacterial ; Humans ; Mutation ; Neisseria meningitidis/genetics ; Neisseria meningitidis/metabolism ; Neisseria meningitidis/pathogenicity ; Phenotype
Chemical Substances	Bacterial Proteins ; Fimbriae Proteins (147680-16-8)
Language	English
Publishing date	2020-11-02
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/s41467-020-19347-y
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